Temat: protease - Katalog OPAC zbiorów

Skocz do pozycji: 1.

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

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Skocz do pozycji: 2.

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

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Skocz do pozycji: 3.

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

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Skocz do pozycji: 4.

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

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Skocz do pozycji: 5.

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

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