Some Properties of Porcine Carboxypeptidase N
- 1 January 1982
- journal article
- research article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 363 (1) , 51-58
- https://doi.org/10.1515/bchm2.1982.363.1.51
Abstract
Some properties of carboxypeptidase N purified from pig serum were investigated. The amino acid composition resembles that of human carboxypeptidase N but differs markedly from that of porcine carboxypeptidase B [EC 3.4.17.2]. 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.This publication has 20 references indexed in Scilit:
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