Some properties of porcine carboxypeptidase N.

Détails

ID Serval
serval:BIB_94C56F872739
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Some properties of porcine carboxypeptidase N.
Périodique
Hoppe-seyler's Zeitschrift Für Physiologische Chemie
Auteur(s)
Juillerat-Jeanneret L., Roth M., Bargetzi J.P.
ISSN
0018-4888[print], 0018-4888[linking]
Statut éditorial
Publié
Date de publication
1982
Volume
363
Numéro
1
Pages
51-58
Langue
anglais
Résumé
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.
Mots-clé
Amino Acids/blood, Animals, Carbohydrates/analysis, Carboxypeptidases/blood, Kinetics, Lysine Carboxypeptidase/blood, Lysine Carboxypeptidase/isolation & purification, Substrate Specificity, Swine
Pubmed
Création de la notice
18/10/2010 10:31
Dernière modification de la notice
20/08/2019 15:57
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