Bovine stomach myosin light chain kinase with a marked discrepancy between its enzyme activity and actomyosin activating effect

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概要

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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.

• 日本学士院の論文

著者

• EBASHI Setsuro

  National Institute for Physiological Sciences

• KUWAYAMA Hideto

  Laboratory of Chemistry, Obihiro University of Agriculture and Veterinary Medicine

• NANKO Chizue

  National Institute for Physiological Sciences

関連論文

• Bovine stomach myosin light chain kinase with a marked discrepancy between its enzyme activity and actomyosin activating effect
• Porcine Skeletal Muscle Dystrophin
• Superprecipitation is a model for in vitro contraction superior to ATPase activity.
• The use of dimethyl sulfoxide(DMSO) for protein fractionation.

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