A new feature of angiotensin-converting enzyme in the brain: hydrolysis of substance P.

Abstract:

:Highly purified rat brain angiotensin-converting enzyme hydrolyzes substance P which contains a C-terminal amino acid with an amidated carboxyl group. The hydrolysis of substance P verified by amino-group fluorometry and by high-performance liquid chromatography is inhibited by captopril, but not by phosphoramidon. The presence of sodium chloride is essential for the hydrolysis. The analyses of cleavage products indicate that the enzyme hydrolyzes substance P between Phe7-Phe8 and Phe8-Gly9 by an endopeptidase action, followed by successive release of dipeptides by a dipeptidyl carboxypeptidase action.

authors

Yokosawa H,Endo S,Ogura Y,Ishii S

doi

10.1016/0006-291x(83)90586-7

subject

Has Abstract

pub_date

1983-10-31 00:00:00

pages

735-42

issue

2

eissn

0006-291X

issn

1090-2104

pii

0006-291X(83)90586-7

journal_volume

116

pub_type

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