Conversion of angiotensin-1 to angiotensin-2 by a latent endothelial cell peptidyl dipeptidase that is not angiotensin-converting enzyme.

Abstract:

:Cultured bovine pulmonary artery endothelial cells contain a second peptidyl dipeptidase, distinct from angiotensin-converting enzyme, present in an inactive form associated with a non-dialyzable inhibitor. Partial purification by glycine affinity chromatography separates enzyme from inhibitor to yield a preparation which hydrolyzes angiotensin-1, bradykinin, substance P, atriopeptin-2, enkephalin and Hip-His-Leu. This enzyme is resistant to inhibition by lisinopril, captopril, thiorphan, phosphoramidon, soybean trypsin inhibitor, PMSF and aminopeptidase and carboxypeptidase inhibitors, but is inhibited by EDTA.

authors

Lanzillo JJ,Dasarathy Y,Stevens J,Fanburg BL

doi

10.1016/s0006-291x(86)80487-9

subject

Has Abstract

pub_date

1986-01-29 00:00:00

pages

770-6

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(86)80487-9

journal_volume

134

pub_type

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