STUDIES ON GLUCORECEPTOR. I. SPECIFIC BINDING OF D-GLUCOSE TO PARTIALLY PURIFIED MEMBRANE OF RAT ISLETS OF LANGERHANS

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Three kinds of plasma membranes in rat islet homogenate were fractionated on sucrose gradient centrifuged at 70000g (F_1 : d^<20>=1.14-1.18,F_2 : d^<20>=1.06-1.12,F_3 : d^<20>=1.02-1.05). Every fraction indicated both enzyme activities of 5'-nucleotidase and ATPase which were typical marker enzymes in pancreatic plasma membrane, and the D-[5-^3H] glucose binding with them were dose-dependently inhibited by D-glucose, but not by L-glucose, D-galactose and 3-O-methyl-D-glucose. The D-[5-^3H] glucose binding with only F_2 fraction was inhibited by D-mannose and D-fructose which could stimulate insulin release (60%), phlorizin inhibited remarkably the binding with F_3 fraction (68%), however, the D-[5-^3H] glucose binding with either F_1 or F_2 fraction was slightly inhibited by preincubation with alloxan (0.2 mg/ml, 37°, 10min) (F_1 : 29%, F_2 : 39%) and that with F_3 fraction was not effective (4%). It was found that the insulin release from the B granules which distributed in the pellet fraction on sucrose gradient centrifuged at 70000g, was induced by the interaction with F_2 fraction. Each maximal capacity of glucose binding site in F_1,F_2 and F_3 fractions was estimated at 3.2,1.0 and 3.2 μmol/mg membrane protein, respectively, from those Scatchard's plots for the glucose binding. Consequently, it was estimated that the membrane which associated with insulin release was contained in F_2 fraction among three fractions from the islet homogenate.
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STUDIES ON GLUCORECEPTOR. I. SPECIFIC BINDING OF D-GLUCOSE TO PARTIALLY PURIFIED MEMBRANE OF RAT ISLETS OF LANGERHANS

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