Studies on a Ca2+- and Cyclic Nucleotide-Independent H1 Histone Kinase Purified from Rabbit Skeletal Muscle
スポンサーリンク
概要
- 論文の詳細を見る
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.
- 鳥取大学の論文
著者
-
Kubota Norika
Department Of Pathological Biochemistry Faculty Of Medicine And Gene Research Center Tottori Univers
-
Kubota Norika
Department Of Paediatrics Tottori Prefectural Kaike Rehabilitation Center For Disabled Children
関連論文
- Case of a mentally retarded child with non-24 hour sleep-wake syndrome caused by deficiency of melatonin secretion
- Phosphory lated Sites of M_r 25,000 Protein, a Putative Protein Phosphatase 2A Modulator, and Phosphorylation of the Synthetic Peptide Containing These Sites by Protein Kinase C^1
- Studies on a Ca2+- and Cyclic Nucleotide-Independent H1 Histone Kinase Purified from Rabbit Skeletal Muscle
- Decreased resting energy expenditure in patients with Duchenne muscular dystrophy