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Wyświetlanie 1-15 z 71
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
Wyświetlanie 1-15 z 71

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