The mechanism of histone activation of the hepatic microsomal glucose-6-phosphatase system: a novel method to assay glucose-6-phosphatase activity.
The mechanism of activation of hepatic microsomal glucose-6-phosphatase (EC 3.1.3.9) by histone 2A has been investigated in both intact and disrupted microsomes. Histone 2A increased the Vmax and decreased the Km of glucose-6-phosphatase in intact microsomes but had no effect on glucose-6-phosphatase activity in disrupted microsomes. Histone 2A was shown to activate glucose-6-phosphatase in intact microsomes by disrupting the membrane vesicles and thereby allowing the direct measurement of the activity of the latent glucose-6-phosphatase enzyme. The study demonstrated that disrupting microsomes with histone 2A is an excellent method for directly assaying glucose-6-phosphatase activity as it poses none of the problems encountered with all of the previously used methods.
Blair
J N
JN
Department of Medicine, Ninewells Hospital and Medical School, University of Dundee, U.K.
Burchell
A
A
D000818:Animals; D019826:Cholic Acid; D002793:Cholic Acids / Q000494:pharmacology; D004789:Enzyme Activation; D005952:Glucose-6-Phosphatase / Q000378:metabolism*; D006657:Histones / Q000494:pharmacology*; D007700:Kinetics; D008862:Microsomes, Liver / Q000201:enzymology*; D051381:Rats; D011919:Rats, Inbred Strains
D002793:Cholic Acids; D006657:Histones; D005952:Glucose-6-Phosphatase; D019826:Cholic Acid