マサバ筋肉ホスホグルコムターゼの特性

概要

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記事区分：原著Two phosphoglucomutases, MK (a) and MK (b), were partly purified from the ordinary (white) muscle of Pacific mackerel, Scomber japonicus, by ammonium sulfate fractionation, ion-exchange chromatography on a CM-Toyopearl column, and Sephacryl S-200 gel filtration. The enzymatic properties of the two enzymes were similar. Both had highest activity in 50 mM Tris-maleate buffer at pH 7.2 and in 50 mM Tris-HCl buffer at pH 8.0. The K_m value for glucose 1-phosphate was 1.0 ×10^<-4> M for both. Activity was inhibited by 3-phosphoglycerate, adenosine monophosphate, and fructose 1,6-bisphosphate, which last caused the most inhibition and was non-competitive with glucose 1-phosphate. In the presence of 50 mM SO^<2->_4, the enzyme had 10 to 27% the activity of the control; the activity was stimulated by 40 to 50% in the presence of 10 mM imidazole. These properties of phosphoglucomutases from Pacific mackerel were comparable to those of a rabbit muscle enzyme.
近畿大学の論文
1993-03-15