コイ筋肉ホスホリラ-ゼキナ-ゼの活性化とリン酸化

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In order to obtain further information on the regulation of glycogen metabolism in fish skeletal muscle, the activation and phosphorylation of carp phosphorylase kinase were investigated by using both carp and rabbit cyclic AMP-dependent protein kinase and compared with those of rabbit phosphorylase kinase. The carp cyclic AMP-dependent protein kinase activated and phosphorylated in a similar fashion as rabbit or carp phosphoryiase kinase, just as the mammalian counterpart does. In the cyclic AMP-dependent kinasc-catalyzed reaction, the carp phosphorylase kinase shows a major difference in the patterns of activation and phosphorylation in that unlike those of rabbit phos-phorylase kinase, no correlation between them could be demonstrated and the enzyme activationwere not significantly affected by the incorporation of phosphate. The 32P incorporation into α andβsubunit of the carp enzyme are 45% and 70%, respectively, as compared with that of each subunit of the rabbit. The pH 6.8 to 8.2 enzyme activity ratio is changed only 1.5-fold from 0.27 to 0.41 following phosphorylation of the carp enzyme. And also, the carp enzyme activity is unaffected by phosphorylase kinase phosphatase. It is characterized that the purified carp phosphorylase kinase exists in a non-activated state having a higher activity ratio of pH 6.8 to 8.2. From these results, it is suggested that phosphorylation-dephosphorylation mechanism may play a new role in the regulation of carp phosphorylase kinase and there may be the modified function of a hormonal control of glycogen metabolism in carp muscle.

コイ筋肉ホスホリラ-ゼキナ-ゼの活性化とリン酸化

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