Human plasma prekallikrein. Immunoaffinity purification and activation to alpha- and beta-kallikrein.
Détails
ID Serval
serval:BIB_2DA1E57A5978
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Human plasma prekallikrein. Immunoaffinity purification and activation to alpha- and beta-kallikrein.
Périodique
Journal of Biological Chemistry
ISSN
0021-9258
Statut éditorial
Publié
Date de publication
01/1986
Peer-reviewed
Oui
Volume
261
Numéro
1
Pages
324-327
Langue
anglais
Résumé
Prekallikrein was purified from human plasma with a final yield of 76% using as the principal step adsorption to immobilized chicken antikallikrein IgY. When purified prekallikrein (3.4 microM) was incubated in the presence of beta-Factor XIIa (0.068 microM) for 5 min at 37 degrees C and pH 7.5, alpha-kallikrein was obtained. Upon prolonged incubation (0.5-28 h), the Mr 52,000 heavy chain of alpha-kallikrein was progressively cleaved, resulting in the formation of beta-kallikrein. The formation of beta-kallikrein was characterized as an autolytic process because it was prevented by specific inhibitors of kallikrein, including aprotinin and antikallikrein antibody but not by corn trypsin inhibitor, an inhibitor specific for beta-Factor XIIa.
Mots-clé
Animals, Antibodies, Aprotinin/pharmacology, Chickens, Chromatography, Affinity, Electrophoresis, Polyacrylamide Gel, Factor XII/antagonists & inhibitors, Factor XIIa, Humans, Immunoglobulins, Immunologic Techniques, Kallikreins/antagonists & inhibitors, Kallikreins/isolation & purification, Molecular Weight, Peptide Fragments/antagonists & inhibitors, Prekallikrein/isolation & purification
Pubmed
Web of science
Création de la notice
25/01/2008 15:28
Dernière modification de la notice
20/08/2019 13:12