Results 171 to 180 of about 122,475 (202)

Action of serine carboxypeptidases on endopeptidase substrates, peptide‐4‐methyl‐coumaryl‐7‐amides

European Journal of Biochemistry, 1985
Carboxypeptidase Y hydrolyzed N‐substituted peptide‐4‐methylcoumarin‐7‐amides (peptide‐NH‐Mec) at pH 7 by releasing 7‐amino‐4‐methylcoumarin (NH2‐Mec) which was then followed by carboxypeptidase action. In particular, a chymotrypsin‐directed substrate, Suc‐Leu‐Leu‐Val‐Tyr‐NH‐Mec, was hydrolyzed by the enzyme with a second‐order rate constant of 7200 ...
S, Kunugi, M, Fukuda, R, Hayashi
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Aeromonas sobria serine protease (ASP): a subtilisin family endopeptidase with multiple virulence activities

Biological Chemistry, 2017
AbstractAeromonas sobriaserine protease (ASP) is secreted fromAeromonas sobria, a pathogen causing gastroenteritis and sepsis. ASP resemblesSaccharomyces cerevisiaeKex2, a member of the subtilisin family, and preferentially cleaves peptide bonds at the C-terminal side of paired basic amino acid residues; also accepting unpaired arginine at the P1site ...
Takahisa, Imamura, Yoji, Murakami, Hidetoshi, Nitta   +2 more
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Classification of sheep abomasal mucosal mast cell proteinase as a serine endopeptidase (EC 3.4.21)

International Journal of Biochemistry, 1988
1. Diisopropylphosphofluoridate (Dip-F) and phenylmethanesulphonylfluoride (Pms-F) are inhibitors of "serine" proteinases, and L-trans-epoxysuccinylleucylamido-(4-guanido)-butane (E-64) is an inhibitor of "thiol" proteinases. The effects of these inhibitors on sheep mast cell proteinase (SMCP) were examined. 2.
D P, Knox, J F, Huntley
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A novel leupeptin-sensitive serine endopeptidase present in normal and malignant rat mammary tissues

Molecular and Cellular Biochemistry, 1990
N-Methyl-N-nitrosourea (MNU)-induced rat mammary adenocarcinomas contain high levels of a novel leupeptin-sensitive serine endopeptidase. Its properties apparently differ from those of other similar endopeptidases reported to be present in various normal and malignant mammalian tissues. The same leupeptinsensitive serine endopeptidase was also detected
I, Eto, M D, Bandy
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[The role of serine endopeptidase in cucumber leaf senescence].

Zhi wu sheng li yu fen zi sheng wu xue xue bao = Journal of plant physiology and molecular biology, 2009
The role of serine endopeptidase in cucumber leaf senescence was studied by using the inhibitor of serine endopeptidase and plant growth regulators (6-BA and ABA) on darkness-induced cucumber leaves. The results showed that the senescence of cucumber leaves were delayed by AEBSF [4-(2-aminoethyl) benzenesulfonyl fluoride hydrochloride], an inhibitor of
Peng, Zhang, Fei, Wang, Lie-Feng, Zhang, Qi, Rui, Lang-Lai, Xu   +4 more
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Serine Endopeptidase Activities of Cowpea Seeds: A Time Course during Development and Germination

Crop Science, 2019
ABSTRACTProteases in plants carry out an essential role in protein turnover during seed development and germination. Cysteine proteases (EC 3.4.22) are well‐known participants of such processes. Serine proteases (EC 3.4.21), however, are far less reported as protagonists during these events.
Nathália B. Lima, Rodrigo M. Lima, Alanna M. Botelho, Érica S. Pontes, Márcio S. T. Pinto, Antônia E. A. Oliveira, Kátia V. S. Fernandes   +6 more
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Purification and characterization of an alkaline serine endopeptidase from a feather-degradingXanthomonas maltophiliastrain

Canadian Journal of Microbiology, 2002
A keratinolytic Xanthomonas maltophilia strain (POA-1), cultured on feather meal broth, using keratin as its sole source of carbon and nitrogen, secretes several extracellular peptidases. The major serine peptidase was purified to homogeneity by a five-step procedure. Its purity was evaluated by capillary zone electrophoresis.
C H, De Toni, M F, Richter, J R, Chagas, J A P, Henriques, C, Termignoni   +4 more
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A serine endopeptidase from cucumber leaves is inhibited by l-arginine, guanidino compounds and divalent cations

Phytochemistry, 2001
An endopeptidase was purified and characterized from green leaves of cucumber (Cucumis sativus L. suyo). The purified enzyme, a basic amino acid-specific endopeptidase with a pI of 5.0, was a monomeric protein of 80 kDa whose pH optimum was 9.5. Inhibitor analysis suggested that it was a serine endopeptidase and contained sulfhydryl groups essential ...
Y, Yamauchi, T, Sugimoto, K, Sueyoshi, Y, Oji, K, Tanaka   +4 more
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Prolyl Endopeptidase and Dipeptidyl Peptidase IV are Distantly Related Members of the Same Family of Serine Proteases

Biological Chemistry Hoppe-Seyler, 1992
Prolyl endopeptidase and dipeptidyl peptidase IV are serine proteases which cleave the peptide bonds at the carboxy group of proline residues. They do not show amino acid sequence homology with the known serine enzymes, but a possible relationship between them has not yet been examined.
L, Polgár, E, Szabo
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Characterization of a kinin inactivating serine endopeptidase H2 (kininase) from human urine using fluorogenic substrates

Immunopharmacology, 1999
We have previously described a kinin-inactivating endopeptidase (H2), which was purified 19-fold from human urine by DEAE-cellulose chromatography and gel filtration. The enzyme was inhibited 100% by PMSF, TPCK and pOHMB. In the present communication, we further characterized this enzyme using the fluorogenic substrates Abz-RPPGFSPFRQ-EDDnp (Abz-BKQ ...
Quinto, BMR, Juliano, L., Juliano, M., Carmona, A. K., Stella, RCR, Casarini, D. E.   +5 more
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