Metabolic stability of the LHRH antagonist antide to cell-surface peptidases.

Abstract:

:The susceptibility to hydrolysis of LHRH and the decapeptide analogue Antide has been compared. The hydrolysis of LHRH by pig kidney brush border membranes is inhibited by phosphoramidon (I50 = 5.6 nM) implicating endopeptidase-24.11 in the initiation of hydrolysis. Under conditions in which LHRH is fully degraded by brush border membranes, Antide was completely resistant to hydrolysis. Similar results were obtained with purified preparations of both endopeptidase-24.11 and angiotensin converting enzyme. These data confirm that the remarkable duration of action of Antide is due principally to its stability to hydrolysis by cell-surface peptidases.

authors

Medeiros Mdos S,Turner AJ,Ljungqvist A,Folkers K

doi

10.1016/0006-291x(91)90884-a

subject

Has Abstract

pub_date

1991-04-15 00:00:00

pages

25-30

issue

1

eissn

0006-291X

issn

1090-2104

pii

0006-291X(91)90884-A

journal_volume

176

pub_type

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