魚類筋肉ミオキナーゼに関する研究-I : コイ筋肉よりミオキナーゼの分離・精製

概要

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Myokinase (ATP: AMP phosphotransferase, EC 2.7.4.3) catalysing the equilibrium among ATP, ADP and AMP, was isolated from the extract of carp muscle by ammonium sulfate fractionation, Sephadex G-75, and by DEAE-cellulose and CM-cellulose column chromatography.The separation of two distinct forms of myokinase into different fractions was brought about by gel filtration on Sephadex G-75. These enzymes were termed myokinase I and myokinase II in order of elution from the column.Myokinase I was further purified by means of DEAE-cellulose column chromatography, while myokinase II was further purified on CM-cellulose columns. These purified myokinase isozymes appeared homogeneous on disc gel electrophoretic analysis.This fact suggested that, in spite of the seeming identity of the substrate specificities of these two enzymes, these two forms of myokinase isozymes are composed of different types of proteins.