Results 181 to 190 of about 16,013 (203)

Characterization of Serine Endopeptidases in Cotyledons of Germinated Vigna mungo Seeds

Journal of Plant Research, 1999
seeds. 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, Takashi Okamoto, Takao Minamikawa   +2 more
openaire   +1 more source

Yeast KEX2 gene encodes an endopeptidase homologous to subtilisin-like serine proteases

Biochemical and Biophysical Research Communications, 1988
Yeast Saccharomyces cerevisiae KEX2 gene previously isolated, was characterized as the gene encoding a calcium-dependent endopeptidase required for processing of precursors of alpha-factor and killer toxin. In this study, we report the amino acid sequence of the KEX2 gene product deduced from nucleotide sequencing.
K, Mizuno, T, Nakamura, T, Ohshima, S, Tanaka, H, Matsuo   +4 more
openaire   +2 more sources

Partial purification and characterization of a serine endopeptidase from rat liver plasma membranes

Biochimica et Biophysica Acta (BBA) - General Subjects, 1986
A 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, F, Gueble-Val, M, Blayau, A, Le Treut, J Y, Le Gall   +4 more
openaire   +2 more sources

Heterozygous variants c.781G>A and c.1066dup ofserine protease 56cause familial nanophthalmos by impairing serine-type endopeptidase activity

British Journal of Ophthalmology, 2022
Background/aimsNanophthalmos is a rare developmental, bilateral, sporadic or hereditary form of microphthalmos. In this study, the heterozygous variants c.781G>A and c.1066dup of thePRSS56gene were identified in two patients with nanophthalmos. This study reports the clinical manifestation and the underlying pathogenic mechanism.MethodsWhole-exome ...
Wei Wu, Jingjie Xu, Houfa Yin, Chenxi Fu, Ke Yao, Xiangjun Chen   +5 more
openaire   +2 more sources

Further Characterization of Endopeptidase H2 a Serine Proteinase from Human Urine

1992
A 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, C E, Fellows, R C, Stella, C A, Sampaio   +3 more
openaire   +2 more sources

The Albicidin Resistance Factor AlbD Is a Serine Endopeptidase That Hydrolyzes Unusual Oligoaromatic-Type Peptides

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, Kretz, Julian, Pesic, Alexander, Kerwat, Dennis, Grätz, Stefan, Royer, Monique, Cociancich, Stéphane, Mainz, Andi, Süssmuth, Roderich   +8 more
openaire   +3 more sources

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
openaire   +2 more sources

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
openaire   +2 more sources

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
openaire   +2 more sources