Invitro and Invivo Phosphorylation of Calpain-Like Protease of Allomyces-Arbuscula
Details
Serval ID
serval:BIB_ECDD186235DA
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Invitro and Invivo Phosphorylation of Calpain-Like Protease of Allomyces-Arbuscula
Journal
Plant Science
ISSN
0168-9452
Publication state
Published
Issued date
1991
Peer-reviewed
Oui
Volume
74
Number
1
Pages
35-44
Notes
Fe752
Times Cited:14
Cited References Count:45
Times Cited:14
Cited References Count:45
Abstract
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.
Keywords
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
Create date
25/01/2008 16:32
Last modification date
20/08/2019 16:14