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Novel substrates for angiotensin I converting enzyme.

作者信息

Hersh L B, Gafford J T, Powers J C, Tanaka T, Erdös E G

出版信息

Biochem Biophys Res Commun. 1983 Jan 27;110(2):654-9. doi: 10.1016/0006-291x(83)91199-3.

DOI:10.1016/0006-291x(83)91199-3
PMID:6301459
Abstract

Homogenous human angiotensin converting enzyme (EC 3.4.15.1) cleaves dipeptides from the C-terminus of substrates containing a free carboxyl group. In this study we demonstrate that peptides containing a C-terminal nitrobenzylamine are also cleaved by the enzyme. The hydrolysis of these substrates is inhibited by the specific converting enzyme inhibitors captopril and MK421 as well as by anti-converting enzyme antibody. Sodium chloride accelerates the rate of hydrolysis forty-fold. The product of the reaction, an amino acid nitrobenzylamide, was identified by thin layer chromatography and high performance liquid chromatography. These results suggest that the carboxyl group is not an absolute requirement for substrate hydrolysis.

摘要

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Cleavage of des-Arg9-bradykinin by angiotensin I-converting enzyme from pig kidney cortex.
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Experientia. 1985 Mar 15;41(3):325-8. doi: 10.1007/BF02004493.
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