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    Wyświetlanie 1-13 z 13
    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:
    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:
    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:
    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 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 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:
    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:
    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:
    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
      Wyświetlanie 1-13 z 13

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