The effect of cleavage by a Crotalus atrox alpha-proteinase fraction on the properties of C1-inhibitor

Détails

ID Serval
serval:BIB_B4159EA8BCFE
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
The effect of cleavage by a Crotalus atrox alpha-proteinase fraction on the properties of C1-inhibitor
Périodique
Toxicon
Auteur⸱e⸱s
Patston  P. A., Qi  M., Schifferli  J. A., Schapira  M.
ISSN
0041-0101 (Print)
Statut éditorial
Publié
Date de publication
01/1995
Volume
33
Numéro
1
Pages
53-61
Notes
Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S. --- Old month value: Jan
Résumé
The effect of cleavage of C1-inhibitor at Pro36 by a Crotalus atrox alpha-proteinase fraction on the properties of this serpin was studied. This truncated C1-inhibitor (des 1-36) was fully active as an inhibitor of kallikrein, beta-factor XIIa, and C1s, and modulated the functions of C1 in a normal manner. Also, the half-life of the truncated protein in the circulation of rabbits, both alone and in complex with C1, was not altered. These results show that shock-like symptoms caused by C. atrox envenomation are not attributable to a deficiency in C1-inhibitor caused by the action of the metalloproteinase in the alpha-proteinase fraction.
Mots-clé
Amino Acid Sequence Animals Complement C1 Inactivator Proteins/*metabolism Crotalid Venoms/analysis/*toxicity *Crotalus Humans Kallikreins/metabolism Metalloendopeptidases/*pharmacology Molecular Sequence Data Rabbits
Pubmed
Web of science
Création de la notice
25/01/2008 15:28
Dernière modification de la notice
20/08/2019 15:22
Données d'usage