Williams, C H and Yamamoto, T and Walsh, D M and Allsop, D (1993) Endopeptidase 3.4.24.11 converts N-1-(R,S)carboxy-3-phenylpropyl-Ala-Ala-Phe-p-carboxyanilide into a potent inhibitor of angiotensin-converting enzyme. Biochemical Journal, 294 (3). pp. 681-684. ISSN 0264-6021
Full text not available from this repository.Abstract
It was reported recently that N-1-(R,S)carboxy-3-phenylpropyl-Ala-Ala-Phe-p-carboxyanilide (CPP-A-A-F-pAB), an inhibitor of endopeptidase 3.4.24.15 (E-24.15), also inhibits angiotensin-converting enzyme (ACE) from rabbit lung. We have found that this compound is without effect on ACE purified from pig kidney, at a concentration some 1000-fold greater than the Ki reported for inhibition of the enzyme from lung. However, preincubation of CPP-A-A-F-pAB with neutral endopeptidase 3.4.24.11 (E-24.11) does result in potent inhibitory effects on ACE. We have shown this to be due to formation of a fragment, CPP-A-A, the structure of which is closely related to ACE inhibitors such as enalaprilat. CPP-A-A was found to be a potent inhibitor of pig ACE. Under the conditions used it had an IC50 value of 1.6 x 10(-8) M, compared with the value obtained for captopril of 7.5 x 10(-10) M. These results have important implications for studies of E-24.15 when using CPP-A-A-F-pAB in vivo or in crude tissue extracts where E-24.11 might also be present.
| Item Type: | Article |
|---|---|
| Journal or Publication Title: | Biochemical Journal |
| Uncontrolled Keywords: | Amino Acid Sequence ; Angiotensin-Converting Enzyme Inhibitors ; Animals ; Chromatography, High Pressure Liquid ; Kidney ; Metalloendopeptidases ; Molecular Sequence Data ; Neprilysin ; Oligopeptides ; Rabbits ; Swine |
| Subjects: | UNSPECIFIED |
| Departments: | Faculty of Health and Medicine > Biomedical & Life Sciences |
| ID Code: | 50845 |
| Deposited By: | ep_importer_pure |
| Deposited On: | 07 Nov 2011 17:01 |
| Refereed?: | Yes |
| Published?: | Published |
| Last Modified: | 26 Jul 2012 19:43 |
| Identification Number: | |
| URI: | http://eprints.lancs.ac.uk/id/eprint/50845 |
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