人尿中丝氨酸蛋白酶内肽酶H2的进一步特性研究。
Further characterization of endopeptidase H2 a serine proteinase from human urine.
作者信息
Casarini D E, Fellows C E, Stella R C, Sampaio C A
机构信息
Disciplina de Nefrologia, Escola Paulista de Medicina, São Paulo, Brazil.
出版信息
Agents Actions Suppl. 1992;38 ( Pt 1):422-9. doi: 10.1007/978-3-0348-7321-5_53.
PMID:1281611
Abstract
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. The enzyme behaves as an oligoendopeptidase.
摘要
一种人尿丝氨酸蛋白酶类胰凝乳蛋白酶可水解肽键
苯丙氨酸-丝氨酸（激肽）；甘氨酸-甘氨酸、亮氨酸-精氨酸、苯丙氨酸-赖氨酸（神经肽）以及谷氨酰胺-谷氨酰胺（P物质）。内肽酶H2对具有4至18个氨基酸残基的寡肽的水解效果优于较大的肽，它不水解激肽原或前脑啡肽。该酶表现为一种寡肽内肽酶。
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