フルテキストファイル
著者
Kubota Norika Department of Pathological Biochemistry, Faculty of Medicine, Tottori University
Akagi Toshie Department of Pathological Biochemistry, Faculty of Medicine, Tottori University
Kueda Kazuhiro Department of Pathological Biochemistry, Faculty of Medicine, Tottori University
Saito Sawako Department of Pathological Biochemistry, Faculty of Medicine, Tottori University
Nanba Eiji Gene Research Center, Tottori University 研究者総覧 KAKEN
Brewster Barry S. Neuromuscular Unit, Royal Postgraduate Medical School, Hammersmith Hospital
Strong Peter N. Neuromuscular Unit, Royal Postgraduate Medical School, Hammersmith Hospital
Hashimoto Eikichi Department of Pathological Biochemistry, Faculty of Medicine, Tottori University
キーワード
H1 histone kinase
microsome
protein kinase C
protein phosphorylation
skeletal muscle (rabbit)
抄録
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.
出版者
Tottori University Faculty of Medicine
資料タイプ
学術雑誌論文
ISSN
1346-8049
書誌ID
AA00892882
掲載誌名
Yonago Acta medica
最新掲載誌名
Yonago Acta medica
41
1
開始ページ
31
終了ページ
44
発行日
1998-03
著者版フラグ
出版社版
著作権表記
Yonago Acta medica 編集委員会
掲載情報
Yonago Acta medica. 1998, 41(1), 31-44
部局名
医学部・医学系研究科・医学部附属病院
言語
英語