| Literature DB >> 7061043 |
L Juillerat-Jeanneret, M Roth, J P Bargetzi.
Abstract
Some properties of carboxypeptidase N purified from pig serum have been investigated. The amino acid composition resembles that of human carboxypeptidase N, but differs markedly from that of porcine carboxypeptidase B. The enzyme contains a mass fraction of 0.1 carbohydrates. Both ester and peptide substrates are hydrolyzed at the same site. Peptide substrates are hydrolyzed if lysine or arginine is the C-terminal amino acid, and provided that the penultimate amino acid is not proline. Argininic acid and epsilon-aminocaproic acid are good inhibitors of the enzyme.Entities:
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Year: 1982 PMID: 7061043 DOI: 10.1515/bchm2.1982.363.1.51
Source DB: PubMed Journal: Hoppe Seylers Z Physiol Chem ISSN: 0018-4888