Insulin sensitivity of liver glycogen synthase b into a conversion.
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.
D000818:Animals; D003921:Diabetes Mellitus, Experimental / Q000201:enzymology*; D005947:Glucose / Q000378:metabolism; D006006:Glycogen Synthase / Q000378:metabolism*; D007328:Insulin / Q000494:pharmacology*; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008297:Male; D006005:Phosphorylases / Q000378:metabolism; D011494:Protein Kinases / Q000494:pharmacology; D051381:Rats
D007328:Insulin; D006005:Phosphorylases; D006006:Glycogen Synthase; D011494:Protein Kinases; D005947:Glucose