Results 181 to 190 of about 20,933 (225)
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Characterization of Serine Endopeptidases in Cotyledons of Germinated Vigna mungo Seeds
Journal of Plant Research, 1999seeds. SEP activity was separated into two isoforms by CM-cellulose column chromatography. These forms, termed SEP-1 and SEP-II, showed endopeptidase activities even at acidic pH, suggesting that SEPs are unique serine endopeptidases, since most serine proteases are optimum at neutral pH.
Tomoki Hosokawa +2 more
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Further Characterization of Endopeptidase H2 a Serine Proteinase from Human Urine
1992A human urine serine proteinase chymotrypsin like hydrolyzes the peptide bonds: Phe-Ser (kinin); Gly-Gly, Leu-Arg, Phe-Lys (neuropeptides) and Gln-Gln (substance P). Endopeptidase H2 hydrolyzes better oligopeptides with 4 to 18 aminoacid residues than larger peptides, it does not hydrolyzes kininogen or proenkephalin.
D E, Casarini +3 more
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Action of serine carboxypeptidases on endopeptidase substrates, peptide‐4‐methyl‐coumaryl‐7‐amides
European Journal of Biochemistry, 1985Carboxypeptidase 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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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 +2 more
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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 +2 more
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Partial purification and characterization of a serine endopeptidase from rat liver plasma membranes
Biochimica et Biophysica Acta (BBA) - General Subjects, 1986A serine endopeptidase was partially purified from rat liver plasma membranes by using a four-step procedure: solubilization with N-lauroylsarcosine; Ultrogel AcA-34 chromatography; CM Affi-Gel blue chromatography; agarose-soybean trypsin inhibitor chromatography.
L, Guenet +4 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, 19881. 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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Role of a serine endopeptidase in the hydrolysis of exogenous cholecystokinin by brain slices
Neuroscience, 1989The participation of a serine endopeptidase, previously shown to be involved in endogenous cholecystokinin inactivation [Rose, Camus and Schwartz (1989) Neuroscience 29, 583-594], in the hydrolysis of various exogenous cholecystokinin peptides was studied with slices from rat cerebral cortex.
A, Camus, C, Rose, J C, Schwartz
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A novel leupeptin-sensitive serine endopeptidase present in normal and malignant rat mammary tissues
Molecular and Cellular Biochemistry, 1990N-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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Journal of the American Chemical Society, 2015
The para-aminobenzoic acid-containing peptide albicidin is a pathogenicity factor synthesized by Xanthomonas albilineans in infections of sugar cane. Albicidin is a nanomolar inhibitor of the bacterial DNA gyrase with a strong activity against various Gram-negative bacteria.
Vieweg, Laura +8 more
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The para-aminobenzoic acid-containing peptide albicidin is a pathogenicity factor synthesized by Xanthomonas albilineans in infections of sugar cane. Albicidin is a nanomolar inhibitor of the bacterial DNA gyrase with a strong activity against various Gram-negative bacteria.
Vieweg, Laura +8 more
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Serine Endopeptidase Activities of Cowpea Seeds: A Time Course during Development and Germination
Crop Science, 2019ABSTRACTProteases 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 +6 more
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