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- W1493892823 abstract "Abstract The interaction between bovine testes calmodulin and rabbit fast skeletal muscle myosin light chain kinase was investigated with the zero-length cross-linking reagent N,N'-dicyclohexylcarbodiimide. A cross-linked product of 110 kDa was produced only in the presence of Ca2+. The reaction mixture was separated on diethylaminoethyl cellulose, and a fraction containing the cross-linked complex of calmodulin and myosin light chain kinase was found to have an elevated kinase activity in the absence of Ca2+, which constituted approximately 50% of the maximally stimulated kinase activity of control, and additional kinase activity in the presence of Ca2+, which constituted the remaining 50% of control activity. Calmodulin added exogenously to the cross-linked complex had no effect on the measured Ca2+ dependence or the maximal extent of kinase activity, which is consistent with the cross-linking of calmodulin in close proximity to a regulatory region of myosin light chain kinase. Moreover, the results are consistent with a mechanism whereby the association of calmodulin is sufficient to stimulate kinase activity and the binding of Ca2+ to bound calmodulin increases catalytic efficiency." @default.
- W1493892823 created "2016-06-24" @default.
- W1493892823 creator A5056688456 @default.
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- W1493892823 date "1989-09-01" @default.
- W1493892823 modified "2023-10-14" @default.
- W1493892823 title "An Enzymatically Active Cross-linked Complex of Calmodulin and Rabbit Skeletal Muscle Myosin Light Chain Kinase" @default.
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- W1493892823 doi "https://doi.org/10.1016/s0021-9258(19)84866-4" @default.
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