Inhibition of ( super(3)H)captopril binding by peptide analog angiotensin converting enzyme inhibitors

Ketomethylene containing peptide analogs, modeled after a snake venom pentapeptide, have been shown to be potent angiotensin converting enzyme inhibitors. Although the most potent compounds are up to five times more potent than captopril in inhibiting angiotensin converting enzyme activity, they are...

Full description

Saved in:
Bibliographic Details
Published inBiochemical and biophysical research communications Vol. 135; no. 3; pp. 770 - 777
Main Authors Toll, L, Almquist, R G
Format Journal Article
LanguageEnglish
Published 01.01.1986
Subjects
captopril
peptidyl dipeptidase A
Online AccessGet full text

Cover

More Information
Summary:Ketomethylene containing peptide analogs, modeled after a snake venom pentapeptide, have been shown to be potent angiotensin converting enzyme inhibitors. Although the most potent compounds are up to five times more potent than captopril in inhibiting angiotensin converting enzyme activity, they are relatively weak inhibitors of ( super(3)H)captopril binding to membrane bound angiotensin converting enzyme. This indicates that inhibition of ( super(3)H)captopril binding and enzymatic activity is due to binding to distinct sites. The results suggest that the inhibitors bind to an additional site on the enzyme distinct from the captopril binding site.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
content type line 23
ObjectType-Feature-1
ISSN:0006-291X