Carboxypeptidase-Type Kininase of Human Kidney and Urine.
Abstract
A carboxypeptidase was partially from purified human urine and a similar or identical enzyme was extracted from a particulate fraction of the kidney. The enzyme cleaved basic C-terminal amino acids of peptides including bradykinin. The inhibition of the human renal/urinary carboxypeptidase was different from that of plasma carboxypeptidase N (kininase I) or pancreatic carboxypeptidase B. The urinary enzyme was not affected by inhibitors of catheptic enzymes or kininase II and has no carboxypeptidase A activity. The urinary/renal carboxypeptidase had a mol wt of 40,000. The urinary carboxypeptidase did not cross-react with antiserum to human pancreatic carboxypeptidase B. These properties distinguish carboxypeptidase of human urine and kidney from plasma carboxypeptidase N and from pancreatic carboxypeptidase B. (Author)
Document Details
- Document Type
- Technical Report
- Publication Date
- May 23, 1980
- Accession Number
- ADA086137
Entities
People
- D. M. Marinkovic
- E. G. Erdos
- I. H. Mills
- P. E. Ward
Organizations
- University of Texas at Austin