Accession Number:

AD0722361

Title:

Characteristics of an Enzyme That Inactivates Angiotensin II (Angiotensinase C).

Descriptive Note:

Technical rept.,

Corporate Author:

OKLAHOMA UNIV MEDICAL CENTER OKLAHOMA CITY

Report Date:

1971-03-22

Pagination or Media Count:

25.0

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

Subject Categories:

  • Biochemistry

Distribution Statement:

APPROVED FOR PUBLIC RELEASE