THE CHYMOTRYPSIN-LIKE ACTIVITY OF HUMAN PROSTATE-SPECIFIC ANTIGEN, GAMMA-SEMINOPROTEIN
THE CHYMOTRYPSIN-LIKE ACTIVITY OF HUMAN PROSTATE-SPECIFIC ANTIGEN, GAMMA-SEMINOPROTEIN
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DOI：
10.1016/0014-5793(87)81151-1
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发表时间：
1987-12-10
期刊：
影响因子：
3.5
通讯作者：
HARA, M
中科院分区：
文献类型：
--
作者：
AKIYAMA, K;NAKAMURA, T;HARA, M
摘要γ-SeminoProtein(γ-Sm)是一种人类前列腺特异性抗原，从其全长氨基酸序列来看，是一种丝氨酸蛋白酶，与激肽释放酶家族具有广泛的同源性。γ-Sm的酶活性被定义为以还原的和三甲基氨基的S-3丙基化溶菌酶和胰岛素氧化的A和B链为底物的类凝乳菌素活性。溶菌酶的-Leu↓丝氨酸肽键被γ-Sm迅速降解。γ-Sm还能降解溶菌酶的-Phe-↓-Glu-和胰岛素B链的-Leu-↓Cys(SO3H)-。这些蛋白质的胰岛素A链和精氨酸基或赖氨酸键根本不被γ-Sm水解。
Abstract γ-Seminoprotein (γ-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 γ-Sm was defined as a chymotypsin-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 γ-Sm. γ-Sm also hydrolyzed the-Phe↓ Glu-of lysozyme and the-Leu↓ Cys (SO 3 H)-of insulin B chain. Insulin A chain and arginyl-or lysyl-linkage of these proteins were not hydrolyzed by γ-Sm at all.