Accession Number:

AD0758018

Title:

Purification of Prolylcarboxypeptidase (Angiotensinase C).

Descriptive Note:

Technical rept.,

Corporate Author:

OKLAHOMA UNIV HEALTH SCIENCES CENTER OKLAHOMA CITY DEPT OF PHARMACOLOGY

Report Date:

1973-03-22

Pagination or Media Count:

13.0

Abstract:

Prolylcarboxypeptidase Angiotensinase C was purified 247-fold from homogenized hog kidney cortex by the sequential application of ammonium sulfate precipitation, DEAE-Sephadex and hydroxyapatite column chromatographies. The enzyme was relatively heat stable and free of cathepsin A contamination. Disc gel electrophoresis revealed only a single band of protein indicating homogeneity. The molecular weight of the enzyme was estimated to be 210,000. The Km of prolylcarboxypeptidase with Bz-Pro-Phe substrate was 0.0013 M. After pretreatment with 2-mercaptoethanol, urea and SDS prolylcarboxypeptidase dissociated to subunits. Author

Subject Categories:

  • Biochemistry

Distribution Statement:

APPROVED FOR PUBLIC RELEASE