CONTINUOUS SPECTROPHOTOMETRIC ASSAY FOR ANGIOTENSIN CONVERTING ENZYME

被引：425

作者：

HOLMQUIST, B ^{[1
]}

BUNNING, P ^{[1
]}

RIORDAN, JF ^{[1
]}

机构：

[1] PETER BENT BRIGHAM HOSP,DIV MED BIOL,BOSTON,MA 02115

来源：

ANALYTICAL BIOCHEMISTRY | 1979年 / 95卷 / 02期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1016/0003-2697(79)90769-3

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Furanacryloyl tripeptides conforming to the known substrate specificity of the angiotensin converting enzyme (dipeptidyl carboxypeptidase, EC 3.4.15.1) have been employed to provide a continuous spectrophotometric assay for this peptidase in the visible region. The assay is based on a blue shift of the absorption spectrum that occurs upon hydrolysis of the substrate to produce a furanacryloyl-blocked amino acid and a dipeptide. Of the various furanacryloyl tripeptides tested, furanacryloyl-l-phenylalanylglyeylglycine exhibits the most suitable characteristics for routine assays of angiotensin converting enzyme. © 1979.

引用

页码：540 / 548

页数：9

共 30 条

[1] SUPERACTIVATION OF THERMOLYSIN BY ACYLATION WITH AMINO-ACID N-HYDROXYSUCCINIMIDE ESTERS [J].