Bovine stomach myosin light chain kinase with a marked discrepancy between its enzyme activity and actomyosin activating effect.
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- EBASHI Setsuro
- National Institute for Physiological Sciences
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- KUWAYAMA Hideto
- Laboratory of Chemistry, Obihiro University of Agriculture and Veterinary Medicine
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- NANKO Chizue
- National Institute for Physiological Sciences
書誌事項
- タイトル別名
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- Bovine stomach myosin light chain kinas
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An attempt was made to confirm and develop the work of Kuwayama et al. (J. Biochem. 104, 862-866, 1988) which showed a significant discrepancy between myosin light chain kinase (MLCK) activity (K-activity) and actomyosin-activating activity (L-activity) of bovine stomach. A simple method of preparing 155 kDa protein identical with MLCK was presented. Preparations thus obtained showed high ratios of the L-activity to the K-activity, the highest being 230. This indicates that a mechanism other than the phosphorylation of light chain plays a crucial role on the molecular level in activating contractile processes of the actomyosin-ATP system.
収録刊行物
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- Proceedings of the Japan Academy. Ser. B: Physical and Biological Sciences
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Proceedings of the Japan Academy. Ser. B: Physical and Biological Sciences 74 (6), 142-144, 1998
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詳細情報 詳細情報について
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- CRID
- 1390282679122488064
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- NII論文ID
- 130000903125
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- NII書誌ID
- AA00785485
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- ISSN
- 13492896
- 03862208
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- NDL書誌ID
- 4547548
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可