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Rapid radioassay for prolylcarboxypeptidase (angiotensinase C)

✍ Scribed by Randal A. Skidgel; Eric Wickstrom; Kenshi Kumamoto; Ervin G. Erdös

Book ID
102985653
Publisher
Elsevier Science
Year
1981
Tongue
English
Weight
570 KB
Volume
118
Category
Article
ISSN
0003-2697

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✦ Synopsis

A simple, sensitive assay for prolylcarboxypeptidase (PCP) is described. It utilizes a radiolabeled substrate, benzyloxycarbonyl-L-prolyl-L-['H)alanine, and the details of its synthesis are also reported here. The hydrolysis of the dipeptide substrate is linear with respect to time or protein concentration until 10% of the substrate has been cleaved. Kinetic analysis yielded a K,,, of 4.7 mM. The assay can be used to measure PCP activity in small amounts of biological fluid, homogenized tissue or cultured cells. Measurements of PCP activity in various cultured human cells showed endothelial cells from umbilical veins to have the highest activity (1625 +-151 nmol/mg/h) followed by endothelial cells from umbilical artery (1017 + 46 nmol/ mg/h), human foreskin fibroblasts (719 f 39 nmol/mg/h), and pulmonary artery endothelial ceiis (352 nmol/mg/h).

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