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Tytuł:
The activity of cathepsin D and alpha-1 antitrypsin in hip and knee osteoarthritis
Autorzy:
Olszewska-Slonina, Dorota
Matewski, Dariusz
Jung, Stanislaw
Olszewski, Krzysztof
Czajkowski, Rafal
Braszkiewicz, Joanna
Wozniak, Alina
Kowaliszyn, Bogna
Powiązania:
https://bibliotekanauki.pl/articles/1039618.pdf
Data publikacji:
2013
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
protease
cathepsin D
alpha 1-antitrypsin
antiprotease
cartilage
osteoarthritis
Opis:
The progress of cartilage decay during joint degeneration is not well monitored with biochemical methods. The role of cathepsin D (CAT-D) in articular cartilage deterioration remains unclear. The aim of this study is to assess the activity of CAT-D and alpha-1 antitrypsin (AAT) in blood in patients with hip or knee osteoarthritis. The activity of CAT-D and AAT in blood serum of 40 women and 21 men with hip or knee osteoarthritis was determined before total joint replacement, on the tenth day after surgery, and once in 54 healthy patients. The preoperative activity of CAT-D in patients with osteoarthritis was lower by 53.6% (11.00 ± 4.54 10-2 nM released tyrosine/mg protein/min, P < 0.001) and after surgery by 55.0% (10.67 ± 4.64 10-2 nM released tyrosine/mg protein/min, P < 0.001) when compared to its activity in healthy patients. There was no significant statistical difference between CAT-D activity before the surgery and its activity on the tenth day after it in the analyzed group (P< 0.496). Simultaneously, the preoperative activity of AAT in the OA (osteoarthritis) patients was by 25.5% (0.93 ± 0.32 mg inhibited trypsin/ml blood serum, P < 0.001) and postoperative was by 44.9% higher (1.26 ± 0.36 mg inhibited trypsin/ml blood serum, P < 0.001) than in healthy patients. The low CAT-D activity in osteoarthritis of big joints is associated with a decrease of cartilage cells during the degenerative process. The higher activity of acute phase protein AAT in OA patients' blood serum confirms the inflammatory component in the osteoarthritis process.
Źródło:
Acta Biochimica Polonica; 2013, 60, 1; 99-106
0001-527X
Pojawia się w:
Acta Biochimica Polonica
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:
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 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:
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:
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:
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:
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:
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:
Effect of selected physico-chemical factors on Baltic herring meat hydrolysis rate and proteolytic enzyme activity
Wpływ niektórych czynników fizykochemicznych na aktywność enzymów proteolitycznych i szybkość hydrolizy białek mięsa śledzia bałtyckiego
Autorzy:
Fik, M.
Sypniewska, L.
Thi, N.P.
Powiązania:
https://bibliotekanauki.pl/articles/1396371.pdf
Data publikacji:
1985
Wydawca:
Instytut Rozrodu Zwierząt i Badań Żywności Polskiej Akademii Nauk w Olsztynie
Tematy:
Baltic herring
proteolytic enzyme
protein autohydrolysis
papin
cathepsin
B-500 protease
Opis:
The effect of some physico-chemical factors on the rate of Baltic herring meat protein autohydrolysis and hydrolysis due to papain and B-500 protease from Bacillus subtilis is reported.
Badano wpływ niektórych czynników fizykochemicznych (pH, temperatura, czas inkubacji, dodatek NaCl) na aktywność enzymów proteolitycznych i szybkość hydrolizy białek mięsa śledzia bałtyckiego. Stwierdzono maksimum aktywności proteinaz mięśniowych w pH 4,2 a proteinaz rozdrobnionej ryby całej w pH 3,7 i 8,3 z tym, że hydroliza w pH 3,7 była intensywniejsza niż w pH 8,3 (rys. 1). W obu przypadkach największą aktywność endogennych enzymów proteolitycznych wykazano w temp. 50°C (rys. 2). Stosowany w charakterze konserwanta chlorek sodu w stężeniach do 10 g na 100 g rozdrobnionej ryby całej powodował nieznaczne hamowanie aktywności enzymów tego surowca po krótkiej hydrolizie i wpływał na nie stymulująco po długim czasie hydrolizy (rys. 3). Większe stężenia NaCl znacznie zmniejszały szybkość hydrolizy białek. W celu zwiększenia szybkości hydrolizy białek ryby całej zastosowano papainę (rys. 4) i proteazę B-500 (rys. 5), z których ta ostatnia, pomimo większego inaktywującego wpływu chlorku sodu, była aktywniejsza niż papaina. Oba preparaty enzymatyczne charakteryzowały się mniejszą podatnością na inaktywujący wpływ NaCl, aniżeli endogenne enzymy proteolityczne surowca. Do hydrolizy śledzia w warunkach przemysłowych spośród tych dwóch preparatów lepiej nadaje się proteaza B-500.
Źródło:
Acta Alimentaria Polonica; 1985, 11, 3; 305-312
0137-1495
Pojawia się w:
Acta Alimentaria 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:
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:
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:
Aktywność metaboliczna grzybni trufli letniej Tuber aestivum/Tuber uncinatum Vittad
Metabolic activity of Tuber aestivum/Tuber uncinatum Vittad mycellium
Autorzy:
Jankiewicz, U.
Russel, S.
Bagińska, E.
Hilszczańska, D.
Powiązania:
https://bibliotekanauki.pl/articles/337774.pdf
Data publikacji:
2015
Wydawca:
Instytut Technologiczno-Przyrodniczy
Tematy:
celulaza
ksylanaza
lakaza
lipaza
proteaza
Tuber aestivum/uncinatum
cellulase
laccase
lipase
protease
xylanase
Opis:
Celem prezentowanych badań było oznaczenie aktywności enzymów wydzielanych do podłoża przez dwie formy trufli letniej: Tuber aestivum i Tuber uncinatum Vittad. W pracy wykazano, że T. aestivum i T. uncinatum uwalniają do podłoża hodowlanego białka enzymatyczne o aktywności: lakazy, proteazy, lipazy oraz celulazy i ksylanazy. Analiza aktywności enzymatycznej w płynnych hodowlach obu form trufli letniej wykazała znaczne różnice biochemiczne pomiędzy nimi. Obserwowano zdecydowanie większą aktywność zewnątrzkomórkowych enzymów u T. aestivum, szczególnie lakazową i peptydazową. Wyniki badań wskazują na różną swoistość substratową lipaz wydzielanych przez te trufle: T. uncinatum syntetyzuje lipazy wykazujące aktywność tylko do octanu p-nitrofenolu, natomiast T. aestivum – także do palmitynianu p-nitrofenolu. W hodowlach obu form trufli wykryto niewielką aktywność celulolityczną i ksylanolityczną. Ksylanazy i celulazy oraz lakazy wydzielane przez grzybnię obu form tych trufli mogą brać udział w procesie zawiązywania symbiozy mykoryzowej.
Truffle have long been appreciated for their culinary value. However, knowledge about their biochemical activity is still insufficient. Therefore, the aim of this study was to preliminarily assess the enzymatic activity of two forms of summer truffle (Tuber aestivum Vittad.). The results showed that studied fungi of the genus truffle (Tuber spp.) – T. aestivum and T. uncinatum secrete extracellular enzymatic proteins with activities of: laccase, protease lipase, cellulase and xylanase. The high activity of the enzyme was observed between 10th and 20th day of truffle cultivation in liquid culture. Higher activity of all tested enzymes was detected in the culture of T. aestivum. Significant differences observed in the level and kind of enzymatic activity might indicate different metabolic activity of studied forms of summer truffle.
Źródło:
Woda-Środowisko-Obszary Wiejskie; 2015, 15, 1; 59-68
1642-8145
Pojawia się w:
Woda-Środowisko-Obszary Wiejskie
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
Wyświetlanie 16-30 z 49

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