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Tytuł:
Evaluation of P1 substrate specificity of staphylococcal SplB protease
Autorzy:
Pustelny, Katarzyna
Stach, Natalia
Wladyka, Benedykt
Dubin, Adam
Dubin, Grzegorz
Powiązania:
https://bibliotekanauki.pl/articles/1039355.pdf
Data publikacji:
2014
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
serine protease
serine protease-like
SplB
Staphylococcus aureus
substrate specificity
Opis:
Staphylococcus aureus is a dangerous human pathogen characterized by growing antibiotic resistance. Virulence of S. aureus relies on a variety of secreted and cell surface associated virulence factors among which certain proteolytic enzymes play an important role. Amid staphylococcal extracellular proteases, those encoded by the spl operon remain poorly characterized, both in terms of enzymology and their physiological role. Initial data demonstrated that Spl proteases exhibit restricted substrate specificity. This study describes development of convenient protein FRET substrates for SplB protease and characterization of the substrate preference of the protease at the P1' position. Kinetic data on hydrolysis of a panel of substrates substituted at the said position is provided.
Źródło:
Acta Biochimica Polonica; 2014, 61, 1; 149-152
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
In silico studies of selected xanthophylls as potential candidates against SARS-CoV-2 targeting main protease (Mpro) and papain-like protease (PLpro)
Autorzy:
Karpiński, T.M.
Kwaśniewski, M.
Ożarowski, M.
Alam, R.
Powiązania:
https://bibliotekanauki.pl/articles/2049355.pdf
Data publikacji:
2021
Wydawca:
Instytut Włókien Naturalnych i Roślin Zielarskich
Tematy:
protease
papain-like protease
xanthophyll
coronavirus
COVID-19
antiviral activity
koronawirus
pandemia
działanie przeciwwirusowe
projektowanie leków wspomagane komputerowo
Opis:
Introduction: The main protease (Mpro) and the papain-like protease (PLpro) are essential for the replication of SARS-CoV-2. Both proteases can be targets for drugs acting against SARS-CoV-2. Objective: This paper aims to investigate the in silico activity of nine xanthophylls as inhibitors of Mpro and PLpro. Methods: The structures of Mpro (PDB-ID: 6LU7) and PLpro (PDB-ID: 6W9C) were obtained from RCSB Protein Data Bank and developed with BIOVIA Discovery Studio. Active sites of proteins were performed using CASTp. For docking the PyRx was used. Pharmacokinetic parameters of ADMET were evaluated using SwissADME and pkCSM. Results: β-cryptoxanthin exhibited the highest binding energy: –7.4 kcal/mol in the active site of Mpro. In PLpro active site, the highest binding energy had canthaxanthin of –9.4 kcal/mol, astaxanthin –9.3 kcal/mol, flavoxanthin –9.2 kcal/mol and violaxanthin –9.2 kcal/mol. ADMET studies presented lower toxicity of xanthophylls in comparison to ritonavir and ivermectin. Conclusion: Our findings suggest that xanthophylls can be used as potential inhibitors against SARS-CoV-2 main protease and papain-like protease.
Źródło:
Herba Polonica; 2021, 67, 2; 1-8
0018-0599
Pojawia się w:
Herba Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
A novel alkaline protease from wild edible mushroom Termitomyces albuminosus
Autorzy:
Zheng, Suyue
Wang, Hexiang
Zhang, Guoqing
Powiązania:
https://bibliotekanauki.pl/articles/1039935.pdf
Data publikacji:
2011
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
alkaline protease
mushroom
Termitomyces albuminosus
purification
Opis:
A protease with a molecular mass of 30 kDa and the N-terminal sequence of GLQTNAPWGLARSS, was isolated from fresh fruiting bodies of the wild edible mushroom Termitomyces albuminosus. The purification protocol included ion exchange chromatography on DEAE-cellulose, Q-Sepharose, SP-Sepharose and FPLC-gel filtration on Superdex 75. The protein was unadsorbed on DEAE-cellulose and Q-Sepharose, but adsorbed on SP-Sepharose. The optimal pH and temperature of the purified enzyme were 10.6 and 60 °C, respectively. The enzyme was stable in the presence of 2 % (v/v) Tween 80 and 4 M urea. More than 80 % of the enzyme activity was retained in 2 % (v/v) Triton X 100, 54 % in 10 mM EDTA and 31 % in 2 % (w/v) SDS. The enzyme was strongly inhibited by phenylmethylsulfonyl fluoride (PMSF), but not inhibited by dithiothreitol (DTT), pepstatin or lima bean trypsin inhibitor suggesting that it was a serine protease but not a trypsin-like one. The protease was inhibited by Hg2+, Cu2+, and Fe3+ ions. The Km and Vmax values of the purified enzyme for casein were 8.26 mg ∙ ml-1 and 0.668 mg ∙ ml-1 ∙ min-1, respectively.
Źródło:
Acta Biochimica Polonica; 2011, 58, 2; 269-274
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
The regulatory role of AtDeg5 chloroplast protease in chronological progression of principal growth stages in Arabidopsis thaliana plants
Autorzy:
Baranek, M.
Lucinski, R.
Jackowski, G.
Powiązania:
https://bibliotekanauki.pl/articles/80598.pdf
Data publikacji:
2013
Wydawca:
Polska Akademia Nauk. Czytelnia Czasopism PAN
Tematy:
conference
serine-type protease
chymotrypsin
thylakoid membrane
photosystem II
protease
chloroplast
Arabidopsis thaliana
ontogenesis
growth stage
Źródło:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology; 2013, 94, 3
0860-7796
Pojawia się w:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
New proteases of the chloroplast envelope – what do they do there?
Autorzy:
Adam, Z.
Powiązania:
https://bibliotekanauki.pl/articles/80681.pdf
Data publikacji:
2013
Wydawca:
Polska Akademia Nauk. Czytelnia Czasopism PAN
Tematy:
conference
protease
chloroplast
thylakoid
proteomics
allene oxide synthase
jasmonic acid
serine protease
Źródło:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology; 2013, 94, 3
0860-7796
Pojawia się w:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Protease purification and characterization of a serine protease inhibitor from Egyptian varieties of soybean seeds and its efficacy against Spodoptera littoralis
Autorzy:
Abd El-latif, A.O.
Powiązania:
https://bibliotekanauki.pl/articles/65779.pdf
Data publikacji:
2015
Wydawca:
Polska Akademia Nauk. Czytelnia Czasopism PAN
Opis:
Serine inhibitors have been described in many plant species and are universal throughout the plant kingdom. Trypsin inhibitors are the most common type. In the present study, trypsin and chymotrypsin inhibitory activity was detected in the seed flour extracts of four Egyptian varieties of soybean (Glycine max). The soybean variety, Giza 22, was found to have higher trypsin and chymotrypsin inhibitory potential compared to other tested soybean varieties. For this reason, Giza 22 was selected for further purification studies which used ammonium sulphate fractionation and DEAE-Sephadex A-25 column. Soybean purified proteins showed a single band on SDS-PAGE corresponding to a molecular mass of 17.9 kDa. The purified inhibitor was stable at temperatures below 60°C and was active at a wide range of pH, from 2 to 12 pH. The kinetic analysis revealed a non-competitive type of inhibition against trypsin and chymotrypsin enzymes. The inhibitor constant (Ki) values suggested that the inhibitor has higher affinity toward a trypsin enzyme than to a chymotrypsin enzyme. Purified inhibitor was found to have deep and negative effects on the mean larval weight, larval mortality, pupation, and mean pupal weight of Spodoptera littoralis. It may be concluded, that soybean protease inhibitor gene(s) could be potential targets for those future studies which are concerned with developing insect resistant transgenic plants.
Źródło:
Journal of Plant Protection Research; 2015, 55, 1
1427-4345
Pojawia się w:
Journal of Plant Protection Research
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Three Pseudomonas aeruginosa strains with different protease profiles
Autorzy:
Andrejko, Mariola
Zdybicka-Barabas, Agnieszka
Janczarek, Monika
Cytryńska, Małgorzata
Powiązania:
https://bibliotekanauki.pl/articles/1039614.pdf
Data publikacji:
2013
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
aprA
alkaline protease
extracellular proteases
elastase B
virulence
lasB
Pseudomonas aeruginosa
Opis:
The proteolytic activity of three Pseudomonas aeruginosa strains, ATCC 27853 - a reference strain, and two clinical isolates was tested. The activity was examined after culturing the bacteria in two different growth media: the minimal M9 medium and rich Luria-Bertani broth (LB). Based on zymograms and protease activity specific assays, it was concluded that the reference strain produced three proteolytic enzymes in the LB medium: protease IV, elastase B and elastase A, while alkaline protease was only produced in the M9 medium. The clinical isolates of P. aeruginosa produced elastase B and alkaline protease when grown in the LB medium and the minimal M9 medium, respectively. PCR analysis confirmed the presence of both the lasB gene encoding elastase B and aprA coding for alkaline protease in the genomes of the three P. aeruginosa strains analyzed. The expression of these genes coding for two important P. aeruginosa virulence factors was dependent on the growth conditions in all the strains studied. The contribution of the extracellular proteinases to the virulence of P. aeruginosa strains used in this study was investigated using an insect model, the greater wax moth Galleria mellonella.
Źródło:
Acta Biochimica Polonica; 2013, 60, 1; 83-90
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Downregulation of chloroplast protease AtDeg5 leads to changes in chronological progression of ontogenetic stages, leaf morphology and chloroplast ultrastructure in Arabidopsis
Autorzy:
Baranek, M.
Wyka, T.P.
Jackowski, G.
Powiązania:
https://bibliotekanauki.pl/articles/57852.pdf
Data publikacji:
2015
Wydawca:
Polskie Towarzystwo Botaniczne
Tematy:
chloroplast protease
AtDeg5 protease
chronological progression
ontogenetic stage
leaf morphology
chloroplast ultrastructure
Arabidopsis
starch grain
Opis:
The chloroplast protein AtDeg5 is a serine-type protease peripherally attached to thylakoid membrane at its lumenal side. Since reliable data regarding the role of AtDeg5 in controlling the course of growth and developmental processes are extremely limited, two independent T-DNA insertional lines with different extent of AtDeg5 reduction were prepared and ontogenesis stage-based analysis performed. Both mutant lines displayed a compensatory overaccumulation of AtDeg8. The repression of AtDeg5 protease altered a range of phenotypic features in at least one of the mutants, with the most prominent being changes in chronological progression of development and growth of individual rosette leaves, flower production and silique ripening as well as in the area of fully expanded leaves and chloroplast ultrastructure. By analyzing the results of parallel-mutant screening we conclude that AtDeg8 overdose may rescue 23% of AtDeg5 deficiency with regard to some AtDeg5-controlled traits; alternatively AtDeg5 may have catalytic sites in excess so that these traits might remain unaltered when AtDeg5 pool is reduced by 23%. For some other AtDeg5-dependent traits the absence of excessive amount of AtDeg5 catalytic sites, lack of AtDeg5 dosage effect and inability of AtDeg8 to compensate deficiency or absence of AtDeg5 occurred.
Źródło:
Acta Societatis Botanicorum Poloniae; 2015, 84, 1
0001-6977
2083-9480
Pojawia się w:
Acta Societatis Botanicorum Poloniae
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
AtDeg2 - a chloroplast protein with dual protease/chaperone activity
Autorzy:
Jagodzik, P.
Adamiec, M.
Jackowski, G.
Powiązania:
https://bibliotekanauki.pl/articles/57301.pdf
Data publikacji:
2014
Wydawca:
Polskie Towarzystwo Botaniczne
Tematy:
chloroplast protein
protease
proteolytic enzyme
chaperone
enzyme activity
chloroplast
PDZ domain
Opis:
Chloroplast protease AtDeg2 (an ATP-independent serine endopeptidase) is cytosolically synthesized as a precursor, which is imported into the chloroplast stroma and deprived of its transit peptide. Then the mature protein undergoes routing to its functional location at the stromal side of thylakoid membrane. In its linear structure AtDeg2 molecule contains the protease domain with catalytic triad (HDS) and two PDZ domains (PDZ1 and PDZ2). In vivo AtDeg2 most probably exists as a supposedly inactive haxamer, which may change its oligomeric stage to form active 12-mer, or 24-mer. AtDeg2 has recently been demonstrated to exhibit dual protease/chaperone function. This review is focused on the current awareness with regard to AtDeg2 structure and functional significance.
Źródło:
Acta Societatis Botanicorum Poloniae; 2014, 83, 3
0001-6977
2083-9480
Pojawia się w:
Acta Societatis Botanicorum Poloniae
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Immobilization of Bacillus megaterium in Carrageenan from Maluku Sea and Their Effect on Protease Production
Autorzy:
Hamdani, Syarif
Nurlatifah, Sri
Astriany, Dewi
Singgih, Marlia W.
Ibrahim, Slamet W.
Powiązania:
https://bibliotekanauki.pl/articles/1811540.pdf
Data publikacji:
2020
Wydawca:
Politechnika Koszalińska. Wydawnictwo Uczelniane
Tematy:
carrageenan
immobilization
protease activity
Bacillus megaterium
Opis:
Bacteria immobilized in carrageenan are widely used in industry to facilitate bacterial handling and storage. Carrageenan is derived from seaweed and its nature is influenced by the condition of the origin of the sea where seaweed grows, one of the Indonesia sea territories that has seaweed that contains caraganen with good properties is Maluku. This study was conducted to determine the effect of storage time of bacteria immobilized in Maluku sea’s carrageenan on proteolytic activity, the bacteria used were Bacillus megaterium. Bacterial immobilization of carrageenan was made at concentrations of 1%, 1.5%, and 2%, storage in cold conditions for up to 9 months. Protease activity was tested using Kunitz method by adding casein as a substrate. The optimal concentration of carrageenan for immobilization of Bacillus megaterium was obtained at a concentration of 1.5%. Protease isolated from immobilized Bacillus megaterium showed increased activity value from storage for 4 months (0.0489 Ug-1) to 7 months (0.1372 Ug-1), and decreased activity after being stored for 9 months (0.0501 Ug-1).
Źródło:
Rocznik Ochrona Środowiska; 2020, Tom 22, cz. 1; 60-69
1506-218X
Pojawia się w:
Rocznik Ochrona Środowiska
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Functional conservation between yeast and plant mitochondrial m-AAA proteases
Autorzy:
Skibior, R.
Kolodziejczak, M.
Janska, H.
Powiązania:
https://bibliotekanauki.pl/articles/80313.pdf
Data publikacji:
2013
Wydawca:
Polska Akademia Nauk. Czytelnia Czasopism PAN
Tematy:
conference
FtsH protease
bifunctional enzyme
ATPase
plant mitochondrion
yeast
AAA protease
Arabidopsis
ribosomal subunit
immunoblotting
biogenesis
Źródło:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology; 2013, 94, 3
0860-7796
Pojawia się w:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Hydroxyapatite as a support in protease immobilization process
Autorzy:
Zdarta, J.
Budzinska, K.
Kolodziejczak-Radzimska, A.
Klapiszewski, Ł.
Siwinska-Stefanska, K.
Bartczak, P.
Piasecki, A.
Maciejewski, H.
Jesionowski, T.
Powiązania:
https://bibliotekanauki.pl/articles/110452.pdf
Data publikacji:
2015
Wydawca:
Politechnika Wrocławska. Oficyna Wydawnicza Politechniki Wrocławskiej
Tematy:
hydroxyapatite
enzyme immobilization
protease
physicochemical characteristic
Opis:
Hydroxyapatite is used as a matrix for immobilization of protease from Aspergillus oryzae by a process of adsorption. The matrix obtained has the surface area of 26 m2/g and particles in the shape of flakes of diameters no greater than 650 nm. The efficiency of the proposed method was confirmed by the Fourier transform infrared spectroscopy, elemental analysis and by analysis of parameters of the pore structure of matrix and products after immobilization. On the basis of the Bradford method it was found that the greatest amount of enzyme (132 mg/g) was immobilized from a solution of initial enzyme concentration of 7 mg/cm3 after 24 h of the process.
Źródło:
Physicochemical Problems of Mineral Processing; 2015, 51, 2; 633-646
1643-1049
2084-4735
Pojawia się w:
Physicochemical Problems of Mineral Processing
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Charakterystyka biochemiczna proteazy syntetyzowanej przez Streptomyces rimosus
Characterization of the protease synthesized by Streptomyces rimosus
Autorzy:
Jankiewicz, U.
Koblak, S.
Wierzchowski, P.
Russel, S.
Powiązania:
https://bibliotekanauki.pl/articles/338007.pdf
Data publikacji:
2018
Wydawca:
Instytut Technologiczno-Przyrodniczy
Tematy:
enzymy proteolityczne
inhibitory proteaz
optimum temperaturowe
promieniowce
Actinomycetes
protease inhibitors
proteolytic enzymes
temperature optimum
Opis:
Badania prezentowane w niniejszej pracy miały na celu charakterystykę biochemiczną zewnątrzkomórkowej proteazy syntetyzowanej przez wyizolowany z gleby szczep Streptomyces rimosus i ocenę możliwości praktycznego wykorzystania tego enzymu w przemyśle. Badany enzym wyizolowano z 7-dniowych hodowli bakterii Streptomyces rimosus. Oczyszczony dwukrotnie enzym wykorzystano do charakterystyki biochemicznej w zakresie optymalnych warunków jego działania oraz wpływu aktywatorów i inhibitorów. Proteaza syntetyzowana przez S. rimosus wykazywała najwyższą aktywność w temperaturze 50°C i pH 7,5 oraz wysoką termostabilność w temperaturze 50°C. Dwuwartościowe jony Zn, Mo, Ni, Cd, Co hamowały aktywność enzymu, natomiast Ca i Mg – aktywowały. Silna inhibicja aktywności enzymu w obecności diizopropylofluorofosforanu (DFP) świadczy o tym, że jest to proteaza serynowa. Aktywność badanego enzymu była stabilna w obecności takich detergentów, jak Triton X-100, Tween 20, Tween 80, bromek heksadecylotrimetyloamoniowy (CTAB) oraz dodecylosiarczanu sodu (SDS).
The research was aimed at isolation and biochemical characterization of the extracellular protease synthesized by the soil Streptomyces rimosus and assessment of the possibilities of practical use of this enzyme in the industry. For this purpose, the test enzyme was isolated from 7 day old culture of S. rimosus. The enzyme two-fold purified was used for biochemical characterization for optimal temperature and pH of activity and activators and inhibitors of activity. The S. rimosus protease showed the highest activity at 50°C and at pH 7.5 and high thermostability at 50°C. Divalent ions such as Zn, Mo, Ni, Cd, Co caused inhibition while Ca and Mg stimulated activity. Strong inhibition of activity in the presence of diisopropylfluorophosphate (DFP) indicates that it is a serine protease. The activity of the test enzyme was stable in the presence of such detergents as Triton X-100, Tween 20, Tween 80, hexadecyl trimethyl ammonium bromide (CTAB) and sodium dodecyl sulfate (SDS).
Źródło:
Woda-Środowisko-Obszary Wiejskie; 2018, 18, 2; 5-14
1642-8145
Pojawia się w:
Woda-Środowisko-Obszary Wiejskie
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
A novel alkaline protease with antiproliferative activity from fresh fruiting bodies of the toxic wild mushroom Amanita farinosa
Autorzy:
Sun, Jian
Zhao, Yongchang
Chai, Hongmei
Wang, Hexiang
Ng, Tzi
Powiązania:
https://bibliotekanauki.pl/articles/1039854.pdf
Data publikacji:
2011
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
alkaline protease
fruiting bodies
purification
mushroom
antiproliferative
Amanita farinosa
Opis:
A novel protease with a molecular mass of 15 kDa was purified from fresh fruiting bodies of the wild mushroom Amanita farinosa. The purification protocol entailed anion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, cation exchange chromatography on SP-Sepharose, and gel filtration by fast protein liquid chromatography on Superdex 75. The protease was unadsorbed on DEAE-cellulose but adsorbed on Affi-gel blue gel and SP-Sepharose. It demonstrated a single 15-kDa band in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS/PAGE) and a 15-kDa peak in gel filtration. The optimal pH and optimal temperature of the protease were pH 8.0 and 65 °C, respectively. Proliferation of human hepatoma HepG2 cells was inhibited by the protease with an IC50 of 25 µM. The protease did not have antifungal or ribonuclease activity.
Źródło:
Acta Biochimica Polonica; 2011, 58, 4; 567-572
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Mitochondrial protease AtFtsH4 affects the level of oxidatively modified proteins in seeds and mitochondria of A. thaliana
Autorzy:
Czarna, M.
Smakowska, E.
Janska, H.
Powiązania:
https://bibliotekanauki.pl/articles/80803.pdf
Data publikacji:
2013
Wydawca:
Polska Akademia Nauk. Czytelnia Czasopism PAN
Tematy:
conference
protein carbonylation
oxidative modification
plant
life cycle
AtFtsH4 protease
seed
mitochondrion
Arabidopsis thaliana
Źródło:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology; 2013, 94, 2
0860-7796
Pojawia się w:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
The total protein content, protein fractions and proteases activities of drone prepupae of Apis mellifera due to varrosis
Autorzy:
Żółtowska, K.
Lipiński, Z.
Dmitryjuk, M.
Powiązania:
https://bibliotekanauki.pl/articles/2146371.pdf
Data publikacji:
2005
Wydawca:
Polskie Towarzystwo Parazytologiczne
Tematy:
protease
protease activity
honey bee
drone prepupa
protein fraction
varrosis
total protein
Varroa destructor
Apis mellifera
protein content
Opis:
The proteins level and activities of acid and alkaline proteases in whole body extracts of drone prepupae of Apis mellifera naturaly infested with Varroa destructor were studied. The infested and a non-infested group did not differ significantly in their total protein content. However, some differences in protein profiles were found. A lack of three protein fractions of moderate and lower molecular weight in infested prepupae was noted. Moreover, some differences in the quantity of protein in most of the fractions were observed. The activity of acid proteases from infested prepupae was lower (p < 0.05) compared with the activity of these proteases from the non-infested one group. The infested drone had higher activity of alkaline proteases than non-infested but this difference was not statisticaly significant.
Źródło:
Wiadomości Parazytologiczne; 2005, 51, 1; 43-47
0043-5163
Pojawia się w:
Wiadomości Parazytologiczne
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
The Effect of Potassium Diformate Addition to the Growth Rate and the Activity of Protease Enzyme of Giant Gourami Fingerlings (Osphronemus goramy Lacepede, 1801)
Autorzy:
Yustiati, Ayi
Nugraha, Algi Azmi
Bioshina, Ibnu Bangkit
Andriani, Yuli
Powiązania:
https://bibliotekanauki.pl/articles/1031523.pdf
Data publikacji:
2020
Wydawca:
Przedsiębiorstwo Wydawnictw Naukowych Darwin / Scientific Publishing House DARWIN
Tematy:
Osphronemus goramy
giant gourami
growth
potassium diformate
protease enzyme
Opis:
This research aims to investigate the effect of adding potassium diformate to commercial feed on the increase of absolute growth rate and the activity of protease enzyme. The research was conducted from July to October 2019 in the Aquaculture Laboratory Faculty of Fisheries and Marine Sciences, Padjadjaran University. The method applied in this research was an experimental method using a Completely Randomized Design (CRD), which consists of four treatments and four replications. The treatments were: (A) without addition of Potassium diformate (control), (B) addition of Potassium diformate by 0.3%, (C) addition of Potassium diformate by 0.5%, and (D) addition Potassium diformate by 0.8%. The test fish were 300 giant gouramis with 4-6 cm in length. The containers used in this research were 16 rearing aquaria with a size of 40 30 40 cm3. The density of studied giant gourami fingerlings was 10 fish per aquarium. The rearing period was 40 days. The feeding rate was 3% from biomass. Water quality parameters (temperature, pH, and dissolved oxygen), the absolute growth rate, feed conversation ratio and survival rate were observed every 10 days. The protease enzyme activities were observed at the end of the research. Data on the absolute growth rate, feeding conversion ratio, the characteristics of protease enzyme and survival rate were analyzed using the Analysis of Variance (ANNOVA) continued with Duncan’s Multiple Range Test at the level of 95%, while the water quality was analyzed descriptively. The results show that the addition of potassium diformate by 0.3% gave the best result with the absolute growth rate of 1.50%, feed conversion ratio of 2.70, protease enzyme activity by 634.2 μ/mL and survival rate of 100%.
Źródło:
World News of Natural Sciences; 2020, 32; 74-86
2543-5426
Pojawia się w:
World News of Natural Sciences
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
The total protein content, protein fractions and proteases activities of drone prepupae of Apis mellifera due to varrosis
Autorzy:
Zoltowska, K
Lipinski, Z.
Dmitryjuk, M.
Powiązania:
https://bibliotekanauki.pl/articles/840749.pdf
Data publikacji:
2005
Wydawca:
Polskie Towarzystwo Parazytologiczne
Tematy:
protease
protease activity
honey bee
drone prepupa
protein fraction
varrosis
total protein
Varroa destructor
Apis mellifera
protein content
Opis:
The proteins level and activities of acid and alkaline proteases in whole body extracts of drone prepupae of Apis mellifera naturaly infested with Varroa destructor were studied. The infested and a non-infested group did not differ significantly in their total protein content. However, some differences in protein profiles were found. A lack of three protein fractions of moderate and lower molecular weight in infested prepupae was noted. Moreover, some differences in the quantity of protein in most of the fractions were observed. The activity of acid proteases from infested prepupae was lower (p < 0.05) compared with the activity of these proteases from the non-infested one group. The infested drone had higher activity of alkaline proteases than non-infested but this difference was not statisticaly significant.
Źródło:
Annals of Parasitology; 2005, 51, 1
0043-5163
Pojawia się w:
Annals of Parasitology
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Binding of Aedes aegypti trypsin modulating oostatic factor [Aea-TMOF] to its receptor stimulates phosphorylation and protease processing of gut-membrane proteins
Autorzy:
Borovsky, D.
Hamdaoui, A.
Powiązania:
https://bibliotekanauki.pl/articles/55079.pdf
Data publikacji:
2008
Wydawca:
Sieć Badawcza Łukasiewicz - Instytut Przemysłu Organicznego
Tematy:
protease processing
Aedes aegypti
electrophoresis
trypsin modulating oostatic factor
phosphorylation
mosquito
insect
larva
gut-membrane protein
fluorography
gut receptor
Opis:
The binding of TMOF to its gut receptor was followed by incubating guts removed from male and female Aedes aegypti. TMOF at physiological concentrations, in the presence of [γ32P]ATP, causes phosphorylation and release of gut-membrane protein (45 kDa) that is further processed by proteolysis. In the presence of protease inhibitors only the 45 kDa protein was released. The phosphorylation and processing of the 45 kDa protein does not happen in the absence of TMOF. Both larvae and adult guts release the protein in the presence of TMOF. Male Ae. aegypti do not synthesize trypsin in their gut and do not release the 45 kDa protein in the presence of TMOF because a TMOF receptor is probably absent. Homogenized guts do not release the 45 kDa protein, indicating that the protease processing or the ecto-protein kinase activity is probably reduced after breaking the tissue. The 45 kDa phosphorylated protein can be dephosphorylated by alkaline phosphatase and protein phosphatase, indicating that the phosphate group is covalently linked to either a serine or a tyrosine moiety. This is the first report that shows that in insects, binding of a peptide hormone activates its receptor by proteolysis.
Źródło:
Pestycydy; 2008, 1-2; 13-25
0208-8703
Pojawia się w:
Pestycydy
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Znaczenie aktywności proteazy kapsydowej CP w rozwoju infekcji alfawirusowych
The role of capsid protease CP activity in the development of alphaviral infections
Autorzy:
Torzyk, Karolina
Skoreński, Marcin
Sieńczyk, Marcin
Powiązania:
https://bibliotekanauki.pl/articles/2200548.pdf
Data publikacji:
2022
Wydawca:
Polskie Towarzystwo Chemiczne
Tematy:
alfawirusy
arbowirusy
proteazy serynowe
proteaza kapsydowa CP
inhibitory
alphaviruses
arboviruses
serine proteases
capsid protease CP
inhibitors
Opis:
Alphaviruses belong to the worldwide distributed Togaviridae family and Alphavirus genus. They are spherical, enveloped, single-stranded RNA arthropodborne viruses. Alphaviruses are mostly transmitted by mosquitoes (Aedes spp. and Anopheles spp.) and are geographically distributed in restricted areas where appropriate vectors are present (Fig.1.). The most recognized members of this genus are Sindbis (SINV), Semliki Forest (SFV), Venezuelan equine encephalitis (VEEV), Ross River (RRV), and Chikungunya (CHIKV) viruses. Alphaviruses are infection agents for humans and many animals. Clinically, most human infections with arthritogenic alphaviruses are associated with symptoms such as fever, headache, joint pain, rash, chronic arthritis, and encephalitis. Major events during the alphaviral infection are virus entry, replication, assembly, and budding of new virions. Alphaviral RNA encodes four nonstructural and five structural proteins. Nonstructural proteins are mainly involved in the replication process and virus pathogenesis, while structural proteins form new virions. Both groups of viral proteins are produced as single polyproteins which undergo autoproteolytic maturation. This process is carried out by the two viral proteases, cysteine protease nsP4 and C protein serine protease (CP), and is considered to be critical for virus replication. The capsid protease CP is a chymotrypsin-like serine protease with the catalytic triad including His145, Asp167, and Ser219. What is important, after a suicidal autoproteolytic event the side chain of Trp267 remains bound in a hydrophobic S1 pocket thus inhibiting further trans-proteolytic activity. Alphaviral capsid protein undergoes a single proteolytic reaction before maturation and then, after selfinactivation, it assembles to form a viral capsid shell. Inhibitors of the capsid protease have significant antiviral activity. Compounds belonging to this group can be good candidates for new antiviral drugs.
Źródło:
Wiadomości Chemiczne; 2022, 76, 5-6; 309--321
0043-5104
2300-0295
Pojawia się w:
Wiadomości Chemiczne
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Extrachromosomal expression of nat05 gene encoding an alkaline serine protease from Bacillus subtilis N05
Autorzy:
Thu, N.T.A.
Chau, N.T.T.
Thien, L.V.
Huy, N.D.
Khue, N.T.M.
Hung, N.B.
Luong, N.N.
Thu, L.T.A.
Loc, N.H.
Powiązania:
https://bibliotekanauki.pl/articles/80935.pdf
Data publikacji:
2018
Wydawca:
Polska Akademia Nauk. Czytelnia Czasopism PAN
Tematy:
gene encoding
serine protease
Bacillus subtilis
nat05 gene
fibrinolytic activity
alkaline serine protease
sodium dodecyl sulphate-polyacrylamide gel electrophoresis
proteolytic enzyme
Źródło:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology; 2018, 99, 4
0860-7796
Pojawia się w:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Defense against own arms: staphylococcal cysteine proteases and their inhibitors.
Autorzy:
Dubin, Grzegorz
Powiązania:
https://bibliotekanauki.pl/articles/1043443.pdf
Data publikacji:
2003
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
staphostatin
staphylococcus
ssp
proteinase
protease inhibitor
staphopain
Opis:
Staphylococcus aureus is a human pathogen causing a wide range of diseases. Most staphylococcal infections, unlike those caused by other bacteria are not toxigenic and very little is known about their pathogenesis. It has been proposed that a core of secreted proteins common to many infectious strains is responsible for colonization and infection. Among those proteins several proteases are present and over the years many different functions in the infection process have been attributed to them. However, little direct, in vivo data has been presented. Two cysteine proteases, staphopain A (ScpA) and staphopain B (SspB) are important members of this group of enzymes. Recently, two cysteine protease inhibitors, staphostatin A and staphostatin B (ScpB and SspC, respectively) were described in S. aureus shedding new light on the complexity of the processes involving the two proteases. The scope of this review is to summarize current knowledge on the network of staphylococcal cysteine proteases and their inhibitors in view of their possible role as virulence factors.
Źródło:
Acta Biochimica Polonica; 2003, 50, 3; 715-724
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
The use of enzymatic fungal activity in the food industry - review
Autorzy:
Drozłowska, Emilia
Powiązania:
https://bibliotekanauki.pl/articles/1076386.pdf
Data publikacji:
2019
Wydawca:
Przedsiębiorstwo Wydawnictw Naukowych Darwin / Scientific Publishing House DARWIN
Tematy:
amylases
enyzmes
fungi
laccase
protease
Opis:
Enzymes are increasingly used in the food industry, due to the fact that they allow to streamline many processes. They catalyse processes that require energy and are long-lasting. Mushrooms produce hydrolytic enzymes such as proteases, lipases and amylases. These enzymes are used in winemaking, brewing, confectionery and cheese production. Attempts have also been made to use paper industry enzymes such as laccase in the wine industry. The production of enzymes of animal origin is an expensive and complicated process, which is why they were interested in their production from microorganisms. This article attempts to review the current state of knowledge on the use of fungal enzymes in the food industry.
Źródło:
World Scientific News; 2019, 116; 222-229
2392-2192
Pojawia się w:
World Scientific News
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Muscle cathepsins of marine fish and invertebrates
Autorzy:
Kolodziejska, I.
Sikorski, Z.E.
Powiązania:
https://bibliotekanauki.pl/articles/1372835.pdf
Data publikacji:
1995
Wydawca:
Instytut Rozrodu Zwierząt i Badań Żywności Polskiej Akademii Nauk w Olsztynie
Tematy:
invertebrate
endopeptidase
fish
structure
protease
extracellular matrix
lysosome
exopeptidase
cathepsin C
cathepsin A
muscle protein
myofibrillar protein
lysosomal protease
marine fish
protein
myofibril
muscle cathepsin
food preservation
sarcoplasm
cathepsin L
carboxypeptidase A
cathepsin B
Opis:
Muscle proteases are located mainly in the lysosomes, in the sarcoplasm, and in the extracellular matrix of the connective tissue surrounding each cell. The lysosomal proteases, cathepsins, have optimum activity in the acidic range, although many of them retain high activity also 1 or 2 pH units away from the optimum value. Among the cathepsins there are endopeptidases and exopeptidases. Most cathepsins hydrolyse several proteins of the myofibrils. The major protease of the lysosomes in fish and squid muscles is cathepsin D, an aspartyl endoproteinase. Although it is present in the muscle fibre itself, its generally rather low activity at low temperature limits its significance in tenderization of refrigerated fish of most species. Cathepsin L, a cysteinyl protease, is involved in autolysis and softening in matured chum salmon. Cathepsin B, a cysteinyl carboxypeptidase, is capable to attack also some myofibrillar proteins. Cathepsin A or carboxypeptidase A, and cathepsin C, a dipeptidyl hydrolase and dipeptidyl transferase, contribute to the hydrolysis of muscle proteins in a concerted action with the other cathepsins.
Źródło:
Polish Journal of Food and Nutrition Sciences; 1995, 04, 3; 3-10
1230-0322
2083-6007
Pojawia się w:
Polish Journal of Food and Nutrition Sciences
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
The use of serine protease from Yarrowia lipolytica yeast in the production of biopeptides from denatured egg white proteins
Autorzy:
Pokora, Marta
Zambrowicz, Aleksandra
Zabłocka, Agnieszka
Dąbrowska, Anna
Szołtysik, Marek
Babij, Konrad
Eckert, Ewelina
Trziszka, Tadeusz
Chrzanowska, Józefa
Powiązania:
https://bibliotekanauki.pl/articles/1038641.pdf
Data publikacji:
2017
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
Yarrowia lipolytica
serine protease
bioactive peptide
antioxidant
ACE-inhibitor
Opis:
Deriving non-conventional enzymes from cheaper sources than those used for commercially available enzymes may result in the production of hydrolysates with beneficial features, while drastically reducing the cost of hydrolysis. This is especially significant for enzymatic hydrolysis as a method of protein waste utilization. We have previously described the ability of non-commercial serine protease from Yarrowia lipolytica yeast to produce/release bioactive peptides from egg white protein by-products (EP). The enzymatic hydrolysis of EP was carried out for 24 h using the serine protease at an enzyme: substrate ratio of 1:30 (w/w). The obtained hydrolysate was characterized by protein degradation of 38% and also exhibited an antioxidant and cytokine-inducing activity. The isolation procedure (ultrafiltration and RP-HPLC) of bioactive peptides from the EP hydrolysate provided peptide fractions with significant antioxidant and ACE inhibitory activities. Three homogeneous and three heterogeneous peptide fractions were identified using MALDI-TOF/MS and the Mascot Search Results database. The peptides, mainly derived from ovalbumin, were composed of 2-19 amino-acid residues. We have thus demonstrated a novel ability of serine protease from Y. lipolytica to release biopeptides from an EP by-product.
Źródło:
Acta Biochimica Polonica; 2017, 64, 2; 245-253
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Mutant HIV-1 Protease Complexed with Tetrapeptide Inhibitor. Preliminary Report
Autorzy:
Skálová, T.
Hašek, J.
Dohnálek, J.
Petroková, H.
Buchtelová, E.
Powiązania:
https://bibliotekanauki.pl/articles/2030577.pdf
Data publikacji:
2002-05
Wydawca:
Polska Akademia Nauk. Instytut Fizyki PAN
Tematy:
87.15.By
Opis:
The paper presents preliminary description of structure determination of a mutant form of HIV-1 protease in a complex with a new pseudotetrapeptide inhibitor that retains its high affinity to this mutant enzyme (A71V, V82T, I84V). A highly efficient microdiffractometer installed for our experiment at the beamline ID14-1 enabled us to collect satisfactory data with crystal dimensions of about 40 micrometers.
Źródło:
Acta Physica Polonica A; 2002, 101, 5; 659-663
0587-4246
1898-794X
Pojawia się w:
Acta Physica Polonica A
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Dengue virus (NS2B/NS3 protease) protein engineering. Part I: An automated design for hotspots stability and site-specific mutations by using HotSpot Wizard 3.0 tool
Autorzy:
Lahiri, Madhumita
Ghosh, Ipsita
Talukdar, Partha
Talapatra, Soumendra Nath
Powiązania:
https://bibliotekanauki.pl/articles/1062840.pdf
Data publikacji:
2019
Wydawca:
Przedsiębiorstwo Wydawnictw Naukowych Darwin / Scientific Publishing House DARWIN
Tematy:
HotSpot Wizard
NS2B/NS3 protease
Non-structural protein
computational tool
protein engineering
Opis:
The non-structural dengue virus (DNV) protein, DNV-2 NS2B/NS3 protease is a combination of two proteins as 2B and 3 and these two proteins in complex replicate faster during dengue fever. The objective of the present study was to detect hot spots and design of smart libraries for engineering protein stability, substrate specificity, tunnels and cavities as well as suitable mutability position of studied protein by using an online tool, HotSpot Wizard (version 3.0). The prediction results were obtained in output interface for functional hot spots, stability hot spots (structural flexibility), correlated hot spots and stability hot spots (sequence consensus) from the sequence string. It is concluded that the prediction of pocket and mutability of this protein can easily be identified the structural alternation especially in disease diagnosis and space for ligand binding site in pocket for the potential of new drug design. Moreover, this computational prediction is suggested to compare with experimental hotspots for studied protein in relation to therapeutic efficacies, which are lacking to prevent viral infection.
Źródło:
World Scientific News; 2019, 127, 3; 177-190
2392-2192
Pojawia się w:
World Scientific News
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Analiza wydajności i specyficzności procesu immobilizacji syntetycznego inhibitora proteaz serynowych z zastosowaniem elektroforezy kapilarnej
Analysis of the efficiency and specificity of the synthetic serine protease inhibitor immobilization process using capillary electrophoresis
Autorzy:
Szałapata, K.
Osińska-Jaroszuk, M.
Grąz, M.
Jarosz-Wilkołazka, A.
Powiązania:
https://bibliotekanauki.pl/articles/2073100.pdf
Data publikacji:
2015
Wydawca:
Stowarzyszenie Inżynierów i Techników Mechaników Polskich
Tematy:
immobilizacja
inhibitor proteaz serynowych AEBSF
elektroforeza kapilarna
immobilization
AEBSF serine protease inhibitor
capillary electrophoresis
Opis:
Przedstawiono proces immobilizacji syntetycznego inhibitora proteaz serynowych AEBSF, który należy do rodziny związków benzosulfonowych. Zastosowanie techniki elektroforezy kapilarnej do celów analizy ilościowej pozwoliło na przeprowadzenie szybkiego pomiaru, charakteryzującego się wysoką specyficznością i precyzją. Na podstawie uzyskanych wyników stwierdzono, że inhibitor AEBSF, poddawany procesowi kowalencyjnej immobilizacji, jest efektywnie wiązany do porowatego nośnika. Jednocześnie określono, że wiąże się on z matrycą także wiązaniami adsorpcyjnymi i hydrofobowymi.
The paper describes a method of immobilization of AEBSF synthetic protease inhibitor which belongs to the family of benzensulfonyl compounds. The application of capillary electrophoresis for a quantitative analysis allows one to perform high-speed measurement characterized by high specificity and repeatability. The obtained results allowed one to confirm that the AEBSF inhibitor under covalent immobilization process is effectively bound to the porous support. It was also determined that AEBSF inhibitor binds to the matrix by adsorption and hydrophobic bonds.
Źródło:
Inżynieria i Aparatura Chemiczna; 2015, 3; 119--120
0368-0827
Pojawia się w:
Inżynieria i Aparatura Chemiczna
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Screening and characterization of Fibrinolytic protease producing Bacillus circulans from mangrove sediments pitchavaram, South East Coast of India
Autorzy:
Sadeesh Kumar, R.
Rajesh, R.
Gokulakrishnan, S.
Subramanian, J.
Powiązania:
https://bibliotekanauki.pl/articles/11234.pdf
Data publikacji:
2015
Wydawca:
Przedsiębiorstwo Wydawnictw Naukowych Darwin / Scientific Publishing House DARWIN
Opis:
Regulation and production of Fibrinolytic enzymes from bacterial sources especially from Bacillus strains has taken a leading role in the medical sciences for the treatment of cardiovascular disorders as it removes thrombus or clots adding to its significant role in curing human health issues saving millions. Significant progress has been made during the last few years on the studies of fibrinolytic enzymes in identifying, cloning, purification, characterization and overproduction of these for commercialization in medical sciences and in fields like detergents development. Production of fibrinolytic enzyme from Bacillus circulans was done using Nutrient broth medium. In addition, a strong fibrinolytic enzyme was purified from the cultivation media. The purified enzyme was almost homogeneous with other species of same genus, as examined by SDS−PAGE and sephadex G-75 column chromatography. The enzyme had an optimal pH of 7-12, an optimal temperature of 50 °C, for fibrin hydrolysis. The molecular mass estimated by gel filtration was 24 to36 KDa. Further studies for characterization and structural elucidation are necessary for their medicinal applications and molecular biological characteristics.
Źródło:
International Letters of Natural Sciences; 2015, 01
2300-9675
Pojawia się w:
International Letters of Natural Sciences
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
3 Noncoding sequences of the CTA 1 gene enhance expression of the recombinant serine protease inhibitor, CPTI II, in Saccharomyces cerevisiae
Autorzy:
Stankiewicz, Magdalena
Rempoła, Bożenna
Fikus, Magdalena
Powiązania:
https://bibliotekanauki.pl/articles/1045124.pdf
Data publikacji:
1996
Wydawca:
Polskie Towarzystwo Biochemiczne
Źródło:
Acta Biochimica Polonica; 1996, 43, 3; 525-529
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Protease Inhibitor from the Crude Extract of Plant Seeds Affects the Digestive Proteases in Hyphantria Cunea (Lep.: Arctiidae)
Autorzy:
Aghaali, N.
Ghadamyari, M.
Hosseininaveh, V.
Riseh, N.S.
Powiązania:
https://bibliotekanauki.pl/articles/66524.pdf
Data publikacji:
2013
Wydawca:
Polska Akademia Nauk. Czytelnia Czasopism PAN
Opis:
Proteases are one of the most important digestive enzymes in the midgut of Hyphantria cunea Drury. Proteases are responsible for protein digestion. In the present study, we evaluated the efficiency of some plant inhibitors on proteases in the gut of the H. cunea. Last instar larvae were collected from mulberry trees. The digestive system of the larvae was used as an enzyme source. The total proteolytic and trypsin activity were assessed by the hemoglobin and BApNA, respectively, as the substrate. The evaluation of the total proteolytic and trypsin activities in various pHs showed the highest relative activity at a pH of 11. Also, the inhibitory effect of inhibitors extracted from Alhagi maurorum Medik., Lathyrus sativus L., Vicia faba L., Prosopis farcta (Banks & Sol.) Eig., and Panicum miliaceum L. on the digestive protease of the fall webworm was measured. Protease inhibitors extracted from A. maurorum, P. farcta and P. miliaceum showed negligible inhibition but L. sativus was able to inhibit 34.72% and 100% of the total activity of proteolytic and trypsin, respectively. Also, the total proteolytic and trypsin activities were inhibited by the inhibitor from V. faba, at 22.27% and 100%, respectively. The zymogram pattern of trypsin with nitro-cellulose membranes showed 2 isoforms in the gut of H. cunea. The inhibitor from L. sativus completely inhibited both isoforms. Gel electrophoresis of proteolitytic activity revealed at least 6 isoforms the inhibitor extracted from L. sativus; completely inhibiting some of them. The inhibitor from L. sativus was purified by ammonium sulfate precipitation and gel-filtration. The molecular mass of the inhibitor was determined as 45 kDa. The highest inhibition of trypsin activity by the inhibitor from L. sativus occurred at a pH of 10. The stability of the inhibitor from L. sativus was evaluated at different pHs and temperatures. The results showed that the inhibitor from L. sativus was stable at a pH of 11.0, and showed 45% inhibition on trypsin activity at a pH of 11. Also, this inhibitor revealed stability up to 50°C.
Źródło:
Journal of Plant Protection Research; 2013, 53, 4
1427-4345
Pojawia się w:
Journal of Plant Protection Research
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Effect of physical and chemical factors in production of alkaline protease enzyme by Bacillus strains
Autorzy:
Tebyanian, H.
Mirhosseiny, S.H.
Bakhtiari, A.
Karami, A.
Dadseresht, S.
Otroshi, B.
Powiązania:
https://bibliotekanauki.pl/articles/11529.pdf
Data publikacji:
2018
Wydawca:
Przedsiębiorstwo Wydawnictw Naukowych Darwin / Scientific Publishing House DARWIN
Źródło:
International Letters of Natural Sciences; 2018, 71
2300-9675
Pojawia się w:
International Letters of Natural Sciences
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Chloroplast protease/chaperone AtDeg2 influences cotyledons opening and reproductive development in Arabidopsis
Autorzy:
Adamiec, M.
Jagodzik, P.
Wyka, T.P.
Ludwikow, A.
Mitula, F.
Misztal, L.
Lucinski, R.
Jackowski, G.
Powiązania:
https://bibliotekanauki.pl/articles/56435.pdf
Data publikacji:
2018
Wydawca:
Polskie Towarzystwo Botaniczne
Opis:
AtDeg2 is a chloroplast protein with dual protease/chaperone activity. Since data on how the individual activities of AtDeg2 affect growth and development of Arabidopsis thaliana plants is missing, two transgenic lines were prepared that express mutated AtDeg2 versions that have either only protease or chaperone activity and a comprehensive ontogenesis stage-based study was performed comprising wild type (WT) plants and insertional mutants that do not express AtDeg2, as well as the two transgenic lines. The repression of both AtDeg2 activities in deg2-3 mutants altered just a few phenotypic traits including the time when cotyledons were fully opened, the time when 10% flowers were open as well as the number of inflorescence branches and seed length in plants which have completed their generative development. It was demonstrated that complete opening of cotyledons as well as the number of inflorescence branches and seed length in plants which have completed their generative development required involvement of both AtDeg2 activities, whereas the time when 10% of flowers were open was controlled by AtDeg2 protease activity. These results show for the first time that the chaperone activity of AtDeg2 is needed for some elements of generative development of A. thaliana plants to proceed normally. So far, the chaperone activity of AtDeg2 was confirmed based on in vitro assays only.
Źródło:
Acta Societatis Botanicorum Poloniae; 2018, 87, 2
0001-6977
2083-9480
Pojawia się w:
Acta Societatis Botanicorum Poloniae
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Gullo’s syndrome – case report
Autorzy:
Rycyk, A.
Furtak, P.
Madro, A.
Kasztelan-Szczerbinska, B.
Cichoz-Lach, H.
Powiązania:
https://bibliotekanauki.pl/articles/2098199.pdf
Data publikacji:
2020
Wydawca:
Instytut Medycyny Wsi
Tematy:
Gullo's syndrome
pancreatic enzyme
lipase
amylase
carcinoembryonic antigen
carbohydrate antigen
serine protease
ultrasonography
Opis:
Benign pancreatic hyperenzymemia (BPH) or Gullo’s Syndrome is a persistent elevation of pancreatic enzymes activity, observed for at least one year, with no pancreatic disorder. This diagnosis is extremely important because it allows us to avoid many unnecessary examinations performed during the diagnostic process. We present a case of a 25-year-old man who was admitted for recurrent elevated lipase and amylase serum values over a time period of 2 years who presented with non-specific abdominal complaints. Interestingly, his routine tests showed sustained elevated serum amylase and lipase activity. He was intensively diagnosed due to pancreatic hyperenzymemia, but no pancreatic disease was detected. The observation lasted two years. The serum lipase and serum amylase levels continued to increase after that time. This diagnosis requires attention because BPH can be the first symptom of pancreatic cancer.
Źródło:
Journal of Pre-Clinical and Clinical Research; 2020, 14, 4; 117-119
1898-2395
Pojawia się w:
Journal of Pre-Clinical and Clinical Research
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Proteolytic activity in the midgut of the crimson speckled moth Utethesia pulchella L. (lepidoptera: arctiidae)
Autorzy:
Ajamhassani, M.
Zibaee, A.
Sendi, J.J.
Askary, H.
Farrar, N.
Powiązania:
https://bibliotekanauki.pl/articles/961656.pdf
Data publikacji:
2012
Wydawca:
Polska Akademia Nauk. Czytelnia Czasopism PAN
Tematy:
utethesia pulchalle
midgut
protease
inhibitor
Opis:
Samples were prepared from the midgut of 4th instar larvae of the crimson speckled moth Utethesia pulchella L. to find proteolytic activity and properties. Result revealed the presence of high proteolytic activity in the midgut when taking into account specific proteinases including trypsin-like, chymotrypsin-like, elastase and two exopeptidase (aminopeptidase and carboxipeptidase). The optimal pH of general protease was 8 and 7 when using azocasein and hemoglobin as general substrates, respectively. The optimal temperature of the total proteolytic activity in the midgut of U. pulchella was 25°C and 30°C when using azocasein and hemoglobin, respectively. Proteolytic activity was inhibited significantly by soybean trypsin inhibitor (SBTI), phenylmethylsulfonyl fluoride (PMSF), trypsin inhibitor (TLCK), chymotrypsin inhibitor (TPCK) and Phenanthroline. These results provide evidences for the presence of serine proteinases as the major proteases in the midgut of U. pulchella; a key rangeland pest in warm climates. The interaction between digestive proteases and protease inhibitors have potentially important consequences for pest management programs.
Źródło:
Journal of Plant Protection Research; 2012, 52, 3
1427-4345
Pojawia się w:
Journal of Plant Protection Research
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Bioactive metabolites produced by Spirulina subsalsa from the Baltic Sea
Autorzy:
Szubert, K.
Wiglusz, M.
Mazur-Marzec, H.
Powiązania:
https://bibliotekanauki.pl/articles/47501.pdf
Data publikacji:
2018
Wydawca:
Polska Akademia Nauk. Instytut Oceanologii PAN
Tematy:
bioactive metabolite
Spirulina subsalsa
Baltic Sea
Cyanoprokaryota
bioremediation
cytotoxic activity
liquid chromatography-tandem mass spectrometry
protease inhibitor
Źródło:
Oceanologia; 2018, 60, 3
0078-3234
Pojawia się w:
Oceanologia
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
New generation of peptide antibiotics
Autorzy:
Dubin, Adam
Mak, Paweł
Dubin, Grzegorz
Rzychon, Małgorzata
Stec-Niemczyk, Justyna
Wladyka, Benedykt
Maziarka, Katarzyna
Chmiel, Dorota
Powiązania:
https://bibliotekanauki.pl/articles/1041366.pdf
Data publikacji:
2005
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
staphostatin
Staphylococcus
virulence factor
hemoglobin
protease inhibitor
hemocidins
antimicrobial agents
antibiotics
Opis:
The increasing antibiotic resistance of pathogenic bacteria calls for the development of alternative antimicrobial strategies. Possible approaches include the development of novel, broad-spectrum antibiotics as well as specific targeting of individual bacterial virulence factors. It is impossible to decide currently which strategy will prove more successful in the future since they both promise different advantages, but also introduce diverse problems. Considering both approaches, our laboratory's research focuses on the evaluation of hemocidins, broad-spectrum antibacterial peptides derived from hemoglobin and myoglobin, and staphostatins, specific inhibitors of staphopains - Staphylococcus aureus secreted proteases that are virulence factors regarded as possible targets for therapy. The article summarizes recent advances in both fields of study and presents perspectives for further development and possible applications.
Źródło:
Acta Biochimica Polonica; 2005, 52, 3; 633-638
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Purification and characterization of a novel metalloprotease from fruiting bodies of Oudemansiella radicata
Autorzy:
Geng, Xueran
Te, Rigen
Tian, Guoting
Zhao, Yongchang
Zhao, Liyan
Wang, Hexiang
Ng, Tzi
Powiązania:
https://bibliotekanauki.pl/articles/1038592.pdf
Data publikacji:
2017
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
edible mushroom
Oudemansiella radicata
protease
purification
Opis:
In this study, a 39-kDa metalloprotease was purified from a rare edible mushroom with health-promoting activities, Oudemansiella radicata, using a purification protocol which entailed anion exchange chromatography on DEAE-cellulose and Q-Sepharose columns and gel filtration by fast protein liquid chromatography on a Superdex 75 column. Some peptide sequences were obtained by LC-MS/MS analysis and one of the sequences, DAWIQADVNR, manifested 90% identity to Coprinopsis cinerea metalloprotease. The optimal reaction pH and temperature for Oudemansiella radicata protease were pH 7.0 and 50°C, respectively. The protease was purified 79-fold and demonstrated a specific protease activity of 2.42 U/mg. The Km of the purified protease for the casein substrate was 0.65 mg/mL at pH 7.0 and 50°C. The activity of the protease was inhibited by Cd2+, Hg2+, Cu2+, Pb2+ and Fe3+ ions, but was enhanced by K+, Mn2+ and Fe2+ ions. The marked suppression of the protease activity by EDTA indicates that the protease is a metalloprotease.
Źródło:
Acta Biochimica Polonica; 2017, 64, 3; 477-483
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Was the serine protease cathepsin G discovered by S. G. Hedin in 1903 in bovine spleen?
Autorzy:
Palesch, David
Sieńczyk, Marcin
Oleksyszyn, Jozef
Reich, Michael
Wieczerzak, Ewa
Boehm, Bernhard
Burster, Timo
Powiązania:
https://bibliotekanauki.pl/articles/1039945.pdf
Data publikacji:
2011
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
spleen cells
Hedin
cathepsin
proteases
Opis:
In the beginning of the 20th century, enzymes with proteolytic activity were classified as peptidases, Erepsin, and proteases. Among these, pepsin, trypsin, and autolytic enzymes were of the protease class. Spleen-derived proteases were poorly characterized until Sven Gustaf Hedin performed several digestion experiments with bovine spleen. He incubated minced bovine spleen under acidic or neutral conditions and characterized two active proteases; the results were published in 1903. The first protease was named α-protease and was active under neutral conditions. The second was named β-protease and was active under acidic conditions. We replicated Hedin's experiments according to his methods and found, by using activity-based probes to visualize proteases, that the historical α-protease is the present-day serine protease cathepsin G (CatG), which is known to be important in several immune processes, including antigen processing, chemotaxis, and activation of surface receptors. The β-protease, however, comprised different proteases including CatX, B, S, and D. We suggest that Hedin described CatG activity in bovine spleen over 100 years ago.
Źródło:
Acta Biochimica Polonica; 2011, 58, 1; 39-44
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Characterization of disulfide exchange between DsbA and HtrA proteins from Escherichia coli
Autorzy:
Skórko-Glonek, Joanna
Sobiecka-Szkatuła, Anna
Lipińska, Barbara
Powiązania:
https://bibliotekanauki.pl/articles/1041221.pdf
Data publikacji:
2006
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
DsbA oxidoreductase
disulfide exchange
HtrA protease
stoichiometry of HtrA-DsbA interaction
kinetics of HtrA oxidation
Opis:
DsbA is the major oxidase responsible for generation of disulfide bonds in proteins of E. coli envelope. In the present work we provided the first detailed characterization of disulfide exchange between DsbA and its natural substrate, HtrA protease. We demonstrated that HtrA oxidation relies on DsbA, both in vivo and in vitro. We followed the disulfide exchange between these proteins spectrofluorimetrically and found that DsbA oxidizes HtrA with a 1 : 1 stoichiometry. The calculated second-order apparent rate constant (kapp) of this reaction was 3.3 × 104 ± 0.6 × 104 M-1s-1. This value was significantly higher than the values obtained for nonfunctional disulfide exchanges between DsbA and DsbC or DsbD and it was comparable to the kapp values calculated for in vitro oxidation of certain non-natural DsbA substrates of eukaryotic origin.
Źródło:
Acta Biochimica Polonica; 2006, 53, 3; 585-589
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Influence of Anisakis simplex stage III larvae upon the activity of proteases under in vitro conditions
Autorzy:
Dziekonska-Rynko, J
Rokicki, J.
Jablonowski, Z.
Powiązania:
https://bibliotekanauki.pl/articles/837165.pdf
Data publikacji:
2002
Wydawca:
Polskie Towarzystwo Parazytologiczne
Tematy:
protease activity
stage
papain
pepsin
trypsin
larva
Anisakis simplex
in vitro
Opis:
The larvae of Anisakis simplex had the largest influence upon decreasing the activity of porcine pepsin. The activity of that enzyme in tests, where the larvae were present during the entire period of incubation, was lower than in the controls. No similar trends were observed in case of the solutions with bovine and porcine trypsin. The activity of those enzymes in the solutions containing the larvae was higher than in the controls. Only the activity of porcine trypsin after 10 h of incubation was slightly lower in the experimental sample than in the control, however, during the later hours the dynamics of the activity decrease of that enzyme in the controls was higher than in the experimental samples. The recorded activity of papain in the samples containing the larvae was higher than that in the controls during the entire time of the experiment.
Źródło:
Annals of Parasitology; 2002, 48, 2
0043-5163
Pojawia się w:
Annals of Parasitology
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Influence of Anisakis simplex stage III larvae upon the activity of proteases under in vitro conditions
Autorzy:
Dziekońska-Rynko, J.
Rokicki, J.
Jabłonowski, Z.
Powiązania:
https://bibliotekanauki.pl/articles/2147699.pdf
Data publikacji:
2002
Wydawca:
Polskie Towarzystwo Parazytologiczne
Tematy:
protease activity
stage
papain
pepsin
trypsin
larva
Anisakis simplex
in vitro
Opis:
The larvae of Anisakis simplex had the largest influence upon decreasing the activity of porcine pepsin. The activity of that enzyme in tests, where the larvae were present during the entire period of incubation, was lower than in the controls. No similar trends were observed in case of the solutions with bovine and porcine trypsin. The activity of those enzymes in the solutions containing the larvae was higher than in the controls. Only the activity of porcine trypsin after 10 h of incubation was slightly lower in the experimental sample than in the control, however, during the later hours the dynamics of the activity decrease of that enzyme in the controls was higher than in the experimental samples. The recorded activity of papain in the samples containing the larvae was higher than that in the controls during the entire time of the experiment.
Źródło:
Wiadomości Parazytologiczne; 2002, 48, 2; 217-223
0043-5163
Pojawia się w:
Wiadomości Parazytologiczne
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Distribution of cathepsin L in human umbilical cord tissues
Autorzy:
Gogiel, Tomasz
Wolańska, Małgorzata
Galewska, Zofia
Kinalski, Piotr
Sobolewski, Krzysztof
Romanowicz, Lech
Powiązania:
https://bibliotekanauki.pl/articles/1038609.pdf
Data publikacji:
2017
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
cathepsin L
cysteine protease inhibitors
umbilical cord
umbilical cord artery
umbilical cord vein
Wharton's jelly
Opis:
The extracellular matrix components show specific distribution patterns within various structures of the umbilical cord, among which Wharton's jelly is especially collagen-rich tissue. Cathepsin L is a potent cysteine protease engaged in degradation of extracellular matrix proteins, including collagens. We evaluated the activity and expression of cathepsin L, and the inhibitory effect of cysteine protease inhibitors in the umbilical cord arteries, vein and Wharton's jelly. Cathepsin L activity and anti-papain inhibitory effect of cysteine protease inhibitors were quantified in extracts of separated umbilical cord tissues using fluorogenic substrates. The results were calculated per DNA content. The enzyme expression was assessed by Western immunoblotting. The active cathepsin L activity (without activation by pepsin digestion), its percentage in the total activity (after pepsin activation), and the expression of the mature single-chain enzyme were the lowest in the umbilical cord arteries and the highest in Wharton's jelly. The effect of cysteine protease inhibitors showed similar distribution as in the case of the active enzyme, being the highest in Wharton's jelly. Distribution of the activity and expression of mature cathepsin L within the umbilical cord probably results from distinctions in the proenzyme activation process. Differences in the action of cysteine protease inhibitors can partly restrict divergences in the enzyme activity that could reflect its expression alone. Differential enzyme action seems to contribute to tissue-specific collagen turnover within the umbilical cord cells, especially those of Wharton's jelly.
Źródło:
Acta Biochimica Polonica; 2017, 64, 3; 507-512
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Theoretical studies of binding modes of two covalent inhibitors of cysteine proteases.
Autorzy:
Drabik, Piotr
Politowska, Ewa
Czaplewski, Cezary
Kasprzykowski, Franciszek
Łankiewicz, Leszek
Ciarkowski, Jerzy
Powiązania:
https://bibliotekanauki.pl/articles/1044228.pdf
Data publikacji:
2000
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
cysteine proteases
covalent protease inhibitors
constrained simulated annealing
papain
molecular dynamics
Opis:
Physiological and pathological roles of cysteine proteases make them important targets for inhibitor development. Although highly potent inhibitors of this group of enzymes are known, their major drawback is a lack of sufficient specificity. Two cysteine protease covalent inhibitors, viz. (i) Z-RL-deoxo-V-peptide-epoxysuccinyl hybrid, and (ii) Z-RLVG-methyl-, have been developed and modeled in the catalytic pocket of papain, an archetypal thiol protease. A number of configurations have been generated and relaxed for each system using the AMBER force field. The catalytic pockets S3 and S4 appear rather elusive in view of the observed inhibitors' flexibility. This suggest rather limited chances for the development of selective structure-based inhibitors of thiol proteases, designed to exploit differences in the structure of catalytic pockets of various members of this family.
Źródło:
Acta Biochimica Polonica; 2000, 47, 4; 1061-1066
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Screening and characterization of thermo-active enzymes of biotechnological interest produced by thermophilic Bacillus isolated from hot springs in Tunisia
Autorzy:
Thebti, Wajdi
Riahi, Yosra
Gharsalli, Rawand
Belhadj, Omrane
Powiązania:
https://bibliotekanauki.pl/articles/1038787.pdf
Data publikacji:
2016
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
temperature
amylase
protease
cellulase
xylanase
mannanase
Geobacillus
Tunisian hot springs
Opis:
As part of the contribution to the global efforts in research of thermostable enzymes being of industrial interest, we focus on the isolation of thermophilic bacteria from Tunisian hot springs. Among the collection of 161 strains of thermophilic Bacillus isolated from different samples of thermal water in Tunisia, 20% are capable of growing at 100°C and the rest grow at 70°C or above. Preliminary activity tests on media supplemented with enzyme-substrates confirmed that 35 strains produced amylases, 37 - proteases, 43 - cellulases, 31 - xylanases and 37 - mannanases. The study of the effect of temperature on enzyme activity led to determination of the optimal temperatures of activities that vary between 60 and 100°C. Several enzymes were active at high temperatures (80, 90 and 100°C) and kept their activity even at 110°C. Several isolated strains producing enzymes with high optimal temperatures of activity were described for the first time in this study. Both strains B62 and B120 are producers of amylase, protease, cellulase, xylanase, and mannanase. The sequencing of 16S DNA identified isolated strains as Geobacillus kaustophillus, Aeribacillus pallidus, Geobacillus galactosidasus and Geobacillus toebii.
Źródło:
Acta Biochimica Polonica; 2016, 63, 3; 581-587
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Body-surface protease inhibitors in cage and hive Apis mellifera L.
Inhibitory proteaz na powierzchni ciała pszczół (Apis mellifera L.) w klatce i w ulu
Autorzy:
Strachecka, A.
Paleolog, J.
Borsuk, G.
Olszewski, K.
Grzywnowicz, K.
Gryzinska, M.
Powiązania:
https://bibliotekanauki.pl/articles/45012.pdf
Data publikacji:
2011
Wydawca:
Zachodniopomorski Uniwersytet Technologiczny w Szczecinie. Wydawnictwo Uczelniane ZUT w Szczecinie
Opis:
The aim of the work was to determine the activity of protease inhibitors sampled from the body surface of bee workers kept in a natural hive environment and in a cage. The samples were collected for five weeks. 40 cage samples and 50 hive samples were gathered, each containing 10 bees. Hydrophilic (water-treated) and hydrophobic (Triton-rinsed) proteins were isolated from the insects. The samples containing washed-out proteins were tested as follows: the activity of aspartic and serine protease inhibitors by the Lee and Lin method; electrophoretic analysis of proteins in a polyacrylamide gel for protease inhibitor detection by means of the modified Felicioli method; and in vivo tests of antifungal and antibacterial activity using the double application method. The cage environment had a destabilizing effect on the natural protease inhibitor system causing radical variation in its activity, which was not the case with the hive environment. The samples were not found to be active in relation to M. luteus and E. coli. The cage bees were less resistant to microorganisms. The results of the in vivo microorganismal test confirmed the fact of weaker protease inhibitor activity in the washed-out body-surface samples of the cage bees that was also observed in in vitro biochemical analyses. The results of cage-based analyses of non-specific apian resistance should be treated with caution when used in reference to hive bees.
Określono aktywność inhibitorów proteaz wyizolowanych z powierzchni ciała robotnic utrzymywanych w naturalnym środowisku ula oraz w klatce. Próby pobierano przez pięć tygodni, pozyskując 40 prób z klatek i 50 prób z ula, w każdej po 10 pszczół. Z owadów wyizolowano białka hydrofilne (przy użyciu wody) oraz hydrofobowe (przy użyciu tritonu). Próbki z wypłukanymi białkami poddano następujący moznaczeniom: aktywność inhibitorów proteaz asparaginowych i serynowych wg metody Lee i Lina; analiza elektroforetyczna białek w żelu poliakrylamidowym do wykrywania inhibitorów proteaz wg zmodyfikowanej metody Felicioliego; aktywność przeciwgrzybowa i antybakteryjna w testach in vivo metodą płytek dwuwarstwowych. Środowisko klatki działało destabilizująco na system naturalnych inhibitorów proteaz wywołując duże wahania ich aktywności, co nie zdarzyło się w ulu. W próbkach nie zaobserwowano aktywności wobec M. luteus i E. coli. Pszczoły w klatce miały słabszą oporność przeciwko mikroorganizmom. Wyniki testu z mikroorganizmami in vivo potwierdziły słabszą aktywność inhibitorów proteaz w próbkach wypłukanych z powierzchni ciał pszczół w klatkach, wykazaną również w analizach biochemicznych in vitro. Uzyskane w klatkach wyniki badań oporności nieswoistej pszczół należy ostrożnie odnosić do pszczół w ulu.
Źródło:
Acta Scientiarum Polonorum. Zootechnica; 2011, 10, 4
1644-0714
Pojawia się w:
Acta Scientiarum Polonorum. Zootechnica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Structure-function relationship of serine protease-protein inhibitor interaction.
Autorzy:
Otlewski, Jacek
Jaskólski, Mariusz
Buczek, Olga
Cierpicki, Tomasz
Czapińska, Honorata
Krowarsch, Daniel
Smalas, Arne
Stachowiak, Damian
Szpineta, Agnieszka
Dadlez, Michał
Powiązania:
https://bibliotekanauki.pl/articles/1044133.pdf
Data publikacji:
2001
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
calorimetry
serine proteases
structural thermodynamics
protein inhibitor
protein-protein recognition
Opis:
We report our progress in understanding the structure-function relationship of the interaction between protein inhibitors and several serine proteases. Recently, we have determined high resolution solution structures of two inhibitors Apis mellifera chymotrypsin inhibitor-1 (AMCI-I) and Linum usitatissimum trypsin inhibitor (LUTI) in the free state and an ultra high resolution X-ray structure of BPTI. All three inhibitors, despite totally different scaffolds, contain a solvent exposed loop of similar conformation which is highly complementary to the enzyme active site. Isothermal calorimetry data show that the interaction between wild type BPTI and chymotrypsin is entropy driven and that the enthalpy component opposes complex formation. Our research is focused on extensive mutagenesis of the four positions from the protease binding loop of BPTI: P1, P1', P3, and P4. We mutated these residues to different amino acids and the variants were characterized by determination of the association constants, stability parameters and crystal structures of protease-inhibitor complexes. Accommodation of the P1 residue in the S1 pocket of four proteases: chymotrypsin, trypsin, neutrophil elastase and cathepsin G was probed with 18 P1 variants. High resolution X-ray structures of ten complexes between bovine trypsin and P1 variants of BPTI have been determined and compared with the cognate P1 Lys side chain. Mutations of the wild type Ala16 (P1') to larger side chains always caused a drop of the association constant. According to the crystal structure of the Leu16 BPTI-trypsin complex, introduction of the larger residue at the P1' position leads to steric conflicts in the vicinity of the mutation. Finally, mutations at the P4 site allowed an improvement of the association with several serine proteases involved in blood clotting. Conversely, introduction of Ser, Val, and Phe in place of Gly12 (P4) had invariably a destabilizing effect on the complex with these proteases.
Źródło:
Acta Biochimica Polonica; 2001, 48, 2; 419-428
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
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