Pz-肽酶和内寡肽酶的活性归因于同一种酶。

Activity of Pz-peptidase and endo-oligopeptidase are due to the same enzyme.

作者信息

Tisljar U, de Camargo A C, da Costa C A, Barrett A J

机构信息

Biochemistry Department, Strangeways Research Laboratory, Cambridge, United Kingdom.

出版信息

Biochem Biophys Res Commun. 1989 Aug 15;162(3):1460-4. doi: 10.1016/0006-291x(89)90838-3.

DOI:10.1016/0006-291x(89)90838-3

PMID:2669752

Abstract

During purification of endo-oligopeptidase from rabbit heart, activities cleaving bradykinin, a substrate of endo-oligopeptidase, and Mcc-Pro-Leu-Gly-Pro-D-Lys(Dnp), a substrate of Pz-peptidase, were found in the same fractions. The hydrolysis of both substrates was inhibited by antisera against endo-oligo-peptidase and Pz-peptidase, and reversibly inhibited by 1, 10-phenanthroline. The purified enzyme hydrolysed Dnp-Pro-Leu-Gly-Pro-Trp-D-Lys, another substrate of Pz-peptidase. Purified Pz-peptidase from rabbit muscle degraded bradykinin and was inhibited by an antiserum against endo-oligopeptidase.

摘要

在从兔心脏中纯化内寡肽酶的过程中，发现能切割内寡肽酶的底物缓激肽以及Pz肽酶的底物Mcc-Pro-Leu-Gly-Pro-D-Lys(Dnp)的活性存在于相同的组分中。两种底物的水解均被抗内寡肽酶和抗Pz肽酶的抗血清所抑制，并被1,10-菲咯啉可逆抑制。纯化的酶能水解Pz肽酶的另一种底物Dnp-Pro-Leu-Gly-Pro-Trp-D-Lys。从兔肌肉中纯化的Pz肽酶能降解缓激肽，并被抗内寡肽酶的抗血清所抑制。