DIPEPTIDYL CARBOXYPEPTIDASE FROM HUMAN SEMINAL PLASMA

被引：41

作者：

DEPIERRE, D ^{[1
]}

BARGETZI, JP ^{[1
]}

ROTH, M ^{[1
]}

机构：

[1] UNIV GENEVA,FAC SCI,DEPT BIOCHIM,CH-1211 GENEVA 4,SWITZERLAND

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1978年 / 523卷 / 02期

关键词：

D O I：

10.1016/0005-2744(78)90049-9

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：

Dipeptidyl carboxypeptidase (angiotensin I converting enzyme) was purified from human seminal plasma. The apparent relative molecular mass determined by gel filtration on Sephadex G-200 was 330 0000. The ptI in isoelectric focusing was 4.6-5.0 and the optimum pH 7.7-8.0. The enzyme is activated by chloride. These properties are similar to those reported for the lung enzyme. The specificity is that of a carboxypeptidase releasing dipeptides. A study of different substrates showed the activity to be highest with Z-Leu-Gly-Gly, followed by Z-Phe-His-Leu > bradykinin > Bz-Gly-Gly-Gly > Boc-Phe-Ala-Pro > Bz-Gly-His-Leu > angiotensin I. © 1978.

引用

页码：469 / 476

页数：8

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