コイ筋肉ホスホリラ-ゼの活性化

概要

論文の詳細を見る
In order to obtain further information on the regulation of glycogen metabolism in fish skeletal muscle, the conversion of carp phosphorylase b into a was investigated and compared with that of rabbit phosphorylase by using both carp and rabbit phosphorylase kinases. Although both the carp and rabbit phosphorylases are phosphorylated and converted to the active form by eitber carp or rabbit phosphorylase kinase, the amount of phosphorylation, the extent of activation and the occurrence of polymerization differed between carp and rabbit phos-phorylase. The carp phosphorylase incorporated one mol of phosphate per 200000g of the enzyme, activated only 50% of the total phosphorylase activity and was not accompanied by a dimerization of the enzyme during the conversion reaction from b to a. From the above results, it is suggested that the carp active phosphorylase is a dimer and a hybrid type containing one phosphorylated and an other non-phosphorylated subunit.