Characteristics of an Enzyme That Inactivates Angiotensin II (Angiotensinase C).
Abstract
Angiotensinase C was partially purified from swine kidney cortex, where it occurs in a lysosomal fraction. The enzyme was also present in human urine, leucocytes and platelets, but absent from red blood cells or plasma. Angiotensinase C breaks bonds of proline at an acid pH provided the imino group of proline is protected and it is in the penultimate position. The C-terminal amino acid liberated from the proline link has to have a free carboxyl group. The substrates include angiotensin II and other peptides. A sensitive fluorometric assay technique was developed based on measuring the amount of DNS-Pro released by the enzyme from the dansylating prolylphenyl-alanine (DNS-Pro-Phe) substrate. The inhibition pattern and substrate specificity indicated that the enzyme is not identical with cathepsins, carboxypeptidases, kininases or other angiotensinases. (Author)
Document Details
- Document Type
- Technical Report
- Publication Date
- Mar 22, 1971
- Accession Number
- AD0722361
Entities
People
- E. G. Erdos
- J. G. Rodgers
- T. A. Jenssen
- T. S. Chiang
- Y. Y. T. Yang
Organizations
- University of Oklahoma