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

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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

Author(s):
Yang, Y. Y. T. ; Erdos, E. G. ; Chiang, T. S. ; Jenssen, T. A. ; Rodgers, J. G.
Author Organization(s):
OKLAHOMA UNIV MEDICAL CENTER OKLAHOMA CITY
Descriptive Note:
Technical rept.,
Pagination:
0025

Security Markings

DOCUMENT & CONTEXTUAL SUMMARY

Distribution:
Approved For Public Release

RECORD

Collection: TR
Identifying Numbers
Report Number(s):
THEMIS-UOMC-TR-38
Contract/Grant Number(s):
N00014-68-A-0496
Project Number(s):
NR-105-516
 Subject Terms
Communities of Interest:
No COI(s) Identified
Descriptor(s):
*ENZYMES, *CARDIOVASCULAR AGENTS, URINE, LEUKOCYTES, BLOOD PLATELETS
Field(s)/Group(s):
Biochemistry
Keyword(s):
*ANGIOTENSIN
Report Date:
1971 Mar 22