PEPTIDE INHIBITORS OF ANGIOTENSIN I-CONVERTING ENZYME IN DIGESTS OF GELATIN BY BACTERIAL COLLAGENASE

被引:139
作者
OSHIMA, G
SHIMABUKURO, H
NAGASAWA, K
机构
[1] School of Pharmaceutical Sciences, Kitasato University, Minato-ku, Tokyo, 108, 5-9-1, Shirokane
关键词
Angiotensin I-converting enzyme; Bradykinin; Collagenase; Gelatin digest; Peptidyldipeptide hydrolase;
D O I
10.1016/0005-2744(79)90255-9
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
Peptide inhibitors of angiotensin I-converting enzyme (peptidyldipeptide hydrolase, EC 3.4.15.1) were produced by digesting gelatin with bacterial collagenase. The inhibitors were isolated from the digests with a combination of alcohol fractionation, treatment with Amberlite CG-50 column, gel filtration through Sephadex G-25, and Dowex 50 column and paper chromatography. Nine peptide fractions were purified to apparent homogeneity judging by thin-layer and ion-exchange column chromatography, and amino acid composition. Amino acid sequences of the peptides were determined: 2 were found to be mixtures of peptides and the sequence of another was only partially determined. Six of the peptides were potent inhibitors of the converting enzyme, while the other three were less active. 6 peptides were substrates for the enzyme. The enzyme released a dipeptide, Ala-Hyp from one peptide and was strongly inhibited by this dipeptide. The remainder of the parent peptides was a less effective inhibitor. © 1979.
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页码:128 / 137
页数:10
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