FEBS Letters | |
The chymotrypsin‐like activity of human prostate‐specific antigen, γ‐seminoprotein | |
Nakamura, Takanori2  Hara, Mitsuwo1  Iwanaga, Sadaaki2  Akiyama, Kazuko1  | |
[1] Department of Legal Medicine, Kurume University School of Medicine, Kurume, Fukuoka 830, Japan;Department of Biology, Faculty of Science, Kyushu University 33, Fukuoka 812, Japan | |
关键词: Prostate-specific antigen; Seminal plasma protease; Chymotrypsin-like enzyme; γ-Seminoprotein; γ-Sm; γ-seminoprotein; RSA-lysozyme; reduced and S-3-(trimethylated amino)propylated lysozyme; pNA; p-nitroanilide; | |
DOI : 10.1016/0014-5793(87)81151-1 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
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 -LeuSer- peptide bond of lysozyme was rapidly hydrolyzed by γ-Sm. γ-Sm also hydrolyzed the -PheGlu- of lysozyme and the -LeuCys(SO3H) -of insulin B chain. Insulin A chain and arginyl- or lysyl-linkage of these proteins were not hydrolyzed by γ-Sm at all.
【 授权许可】
Unknown
【 预 览 】
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