Insulin sensitivity of liver glycogen synthase b into a conversion

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.