A DIPEPTIDYL CARBOXYPEPTIDASE THAT CONVERTS ANGIOTENSIN I AND INACTIVATES BRADYKININ.
Abstract
While studying the inactivation of bradykinin, it was noticed that in addition to carboxypeptidase N, a second enzyme, kininase II, cleaved the peptide. The latter enzyme hydrolyzed the Pro7-Phe8 gond in bradykinin and thus liberated the C-terminal phenylalanylarginine dipeptide. Because kininase II acted as a dipeptidyl carboxypeptidase (DCP), a study was made of its relation to the angiotensin I converting enzyme that liberates a histidylleucine dipeptide from the decapeptide and thereby converts it into the active octapeptide angiotensin II. (Author)
Document Details
- Document Type
- Technical Report
- Publication Date
- Jun 23, 1970
- Accession Number
- AD0709424
Entities
People
- E. G. Erdos
- H. Y. T. Yang
- Y. Levin
Organizations
- University of Oklahoma