File
Authors
Keywords
H1 histone kinase
microsome
protein kinase C
protein phosphorylation
skeletal muscle (rabbit)
Abstract
In an attempt to elucidate the regulatory mechanism of microsomal function by protein phosphorylation, one of the major protein kinases obtained during the preparation of the microsomal fraction of rabbit skeletal muscle was partially purified and characterized. This enzyme was a protein serine/threonine kinase and showed similar, but not completely same properties as those of Ca 2+-phospholipid-dependent protein kinase (protein kinase C), judging from its elution profile from an anion-exchange column, molecular mass, responses to protein kinase activators or inhibitors and the substrate specificity. These results suggest a possible implication of this Ca 2+- and cyclic nucleotide-independent H1 histone kinase in protein phosphorylation of microsomal protein(s), although the exact role and the mechanism of regulation of this enzyme are not clear at this time.
Publisher
Tottori University Faculty of Medicine
Content Type
Journal Article
ISSN・ISBN
1346-8049
NCID
AA00892882
Journal Title
Yonago Acta medica
Current Journal Title
Yonago Acta medica
Volume
41
Issue
1
Start Page
31
End Page
44
Published Date
1998-03
Text Version
Publisher
Rights
Yonago Acta medica 編集委員会
Citation
Yonago Acta medica. 1998, 41(1), 31-44
Department
Faculty of Medicine/Graduate School of Medical Sciences/University Hospital
Language
English