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.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Medeiros Mdos S,Turner AJ,Ljungqvist A,Folkers Kdoi
10.1016/0006-291x(91)90884-asubject
Has Abstractpub_date
1991-04-15 00:00:00pages
25-30issue
1eissn
0006-291Xissn
1090-2104pii
0006-291X(91)90884-Ajournal_volume
176pub_type
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