Article: article from journal or magazin.
Some properties of porcine carboxypeptidase N.
Hoppe-seyler's Zeitschrift Für Physiologische Chemie
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.
Amino Acids/blood, Animals, Carbohydrates/analysis, Carboxypeptidases/blood, Kinetics, Lysine Carboxypeptidase/blood, Lysine Carboxypeptidase/isolation & purification, Substrate Specificity, Swine
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