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- W2980297639 abstract "Abstract A new method to determine calmodulin (CM) activity from the grade of phosphorylation of myosin p-light chain was introduced. By this method the inhibitory action of Ca-antagonists to CM was examined in comparison with the action of CM inhibitors. Phosphorylation was measured from the gel pattern of p-light chain on urea gel electrophoresis of glycerol-treated myosin B which contained the endogeneous light chain kinase and CM, but not phosphatase. The grade of phosphorylation was quantitatively determined from densitometry of the phosphorylated and un- or dephosphorylated p-light chain on the urea gel electro-phoresis. Drugs were added to the myosin B solution before incubation with ATP, and their inhibitory action was determined from the grade of phosphorylation. The drug concentrations required for 50% inhibition of phosphorylation under the incubation for 5 min. were about ImM for Ca-antagonists and around 100μM for CM-inhibitors, respectively. These inhibitory effects of the drugs were suppressed completely by the addition of CM at about 2μM. From these results, it is suggested that Ca antagonists bind to CM and inhibit the complex formation of light chain kinase and Ca-CM, though its ability is less than that of CM-inhibitors." @default.
- W2980297639 created "2019-10-18" @default.
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- W2980297639 date "1983-01-01" @default.
- W2980297639 modified "2023-10-03" @default.
- W2980297639 title "Inhibitory action of Ca-antagonists to calmodulin" @default.
- W2980297639 doi "https://doi.org/10.1016/s0021-5198(19)60481-6" @default.
- W2980297639 hasPublicationYear "1983" @default.
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