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人前列腺特异性抗原γ-精浆蛋白的类胰凝乳蛋白酶活性

The chymotrypsin-like activity of human prostate-specific antigen, gamma-seminoprotein.

作者信息

Akiyama K, Nakamura T, Iwanaga S, Hara M

机构信息

Department of Legal Medicine, Kurume University School of Medicine, Fukuoka, Japan.

出版信息

FEBS Lett. 1987 Dec 10;225(1-2):168-72. doi: 10.1016/0014-5793(87)81151-1.

Abstract

gamma-Seminoprotein (gamma-Sm) is a human prostate-specific antigen and a serine protease judging from the complete amino acid sequence which shows extensive homology with the kallikrein family. The enzymatic activity of gamma-Sm was defined as a chymotrypsin-like activity using reduced and S-3-(trimethylated amino)propylated lysozyme and insulin-oxidized A and B chains as substrates. The -Leu/Ser- peptide bond of lysozyme was rapidly hydrolyzed by gamma-Sm. gamma-Sm also hydrolyzed the -Phe/Glu- of lysozyme and the -Leu/Cys(SO3H)- of insulin B chain. Insulin A chain and arginyl- or lysyl-linkage of these proteins were not hydrolyzed by gamma-Sm at all.

摘要

γ-精蛋白(γ-Sm)是一种人前列腺特异性抗原,从其完整氨基酸序列判断它是一种丝氨酸蛋白酶,该序列与激肽释放酶家族具有广泛的同源性。使用还原型和S-3-(三甲基化氨基)丙基化溶菌酶以及胰岛素氧化的A链和B链作为底物,γ-Sm的酶活性被定义为类似胰凝乳蛋白酶的活性。溶菌酶的-Leu/Ser-肽键被γ-Sm迅速水解。γ-Sm还能水解溶菌酶的-Phe/Glu-以及胰岛素B链的-Leu/Cys(SO3H)-。γ-Sm根本不会水解这些蛋白质的胰岛素A链以及精氨酰或赖氨酰连接键。

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