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The chymotrypsin‐like activity of human prostate‐specific antigen, γ‐seminoprotein
Author(s) -
Akiyama Kazuko,
Nakamura Takanori,
Iwanaga Sadaaki,
Hara Mitsuwo
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)81151-1
Subject(s) - lysozyme , chymotrypsin , biochemistry , chemistry , serine protease , hydrolysis , peptide , peptide bond , kallikrein , protease , peptide sequence , amino acid , catalytic triad , serine , enzyme , trypsin , microbiology and biotechnology , biology , gene
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.