Chum salmon trypsin-catalyzed peptide synthesis with inverse substrates as acyl donor components at low temperature

被引：10

作者：

Sekizaki, H ^{[1
]}

Murakami, M ^{[1
]}

Itoh, K ^{[1
]}

Toyota, E ^{[1
]}

Tanizawa, K ^{[1
]}

机构：

[1] Hlth Sci Univ Hokkaido, Fac Pharmaceut Sci, Ishikari, Hokkaido 0610293, Japan

来源：

JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC | 2000年 / 11卷 / 01期

基金：

日本学术振兴会;

关键词：

chum salmon trypsin; enzymatic peptide synthesis; inverse substrate; N-alpha-(tert-butyloxycarbonyl)amino acid p-amidinophenyl ester; oligopeptide;

D O I：

10.1016/S1381-1177(00)00192-2

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Chum salmon trypsin-catalyzed peptide synthesis has been studied by using p-amidinophenyl esters of N-alpha-(tert-butyloxycarbonyl)amino acid as the acyl donor components at 0 degreesC. The reaction conditions were optimized for an organic solvent, pH, and concentration of the acyl acceptor. The method was shown to be successful as a general method for the synthesis of the peptide, and also useful for the preparation of peptides containing D-amino acids. The enzymatic hydrolysis of the resulting products was negligible. (C) 2000 Elsevier Science B.V. All rights reserved.

引用

页码：23 / 28

页数：6