Purification of Prolylcarboxypeptidase (Angiotensinase C)

摘要

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)