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
Personal Author(s) : Kakimoto,T. ; Oshima,G. ; Yeh,H. S. J. ; Erdos,E. G.
Report Date : 22 MAR 1973
Pagination or Media Count : 13
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)
Descriptors : (*ENZYMES, PURIFICATION), CHROMATOGRAPHIC ANALYSIS, ELECTROPHORESIS
Subject Categories : Biochemistry
Distribution Statement : APPROVED FOR PUBLIC RELEASE