Invitro and Invivo Phosphorylation of Calpain-Like Protease of Allomyces-Arbuscula

Détails

ID Serval
serval:BIB_ECDD186235DA
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Invitro and Invivo Phosphorylation of Calpain-Like Protease of Allomyces-Arbuscula
Périodique
Plant Science
Auteur⸱e⸱s
Ojha  M., Favre  B.
ISSN
0168-9452
Statut éditorial
Publié
Date de publication
1991
Peer-reviewed
Oui
Volume
74
Numéro
1
Pages
35-44
Notes
Fe752
Times Cited:14
Cited References Count:45
Résumé
The calpain-like protease from Allomyces arbuscula was phosphorylated in vitro by a serine/threonine protein kinase from Neurospora crassa typical of casein kinase II. The protease contained covalently bound phosphate when the culture was labelled in vivo with P-32i. The phosphoryl linkage was sensitive to alkaline phosphatase. Phosphoserine was the major phosphohydroxylamino acid detected after acid hydrolysis of the in vitro and in vivo phosphorylated enzyme. Phosphopeptide maps of the protease phosphorylated either in vitro or in vivo were similar. These data suggest that in vivo the protease may be regulated by phosphorylation-dephosphorylation mechanisms.
Mots-clé
allomyces-arbuscula calpain-like protease protein phosphorylation calcium-dependent proteases activated neutral protease kinase-c ca-2+-dependent proteinase endogenous inhibitor cdna clones purification brain identification susceptibility
Web of science
Création de la notice
25/01/2008 17:32
Dernière modification de la notice
20/08/2019 17:14
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