Insulin sensitivity of liver glycogen synthase b into a conversion |
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Authors: | Alvin H. Gold David Dickemper Doris M. Haverstick |
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Affiliation: | (1) Department of Pharmacology, St. Louis University School of Medicine, 63104 St. Louis, Missouri |
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Abstract: | Summary 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.Supported by NIH Grants HD-07788, AM-21149 and, in part, by grants from the Greater St. Louis Diabetic Childrens Welfare Association and the American Diabetes Association, N.Y. |
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