Insulin sensitivity of liver glycogen synthase b into a conversion.
A H Gold, D Dickemper, D M Haverstick
文献索引:Mol. Cell Biochem. 25(1) , 47-59, (1979)
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摘要
Liver glycogen synthase b phosphatase, chromatographically separable from phosphorylase a phosphatase, is decreased in 48-hour alloxan diabetic rats. The phosphatase activities are measured in an in vitro system using exogenous isolated phospho-enzyme as substrates with added phosphatases. Synthase and phosphorylase phosphatases were shown to have differential catalytic properties by their reactivity in the presence of Pi, the heat-stable inhibitor of phosphorylase phosphatase and after incubation with added cAMP-dependent protein kinase.
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