Abstract
Homogenates of either rat or mouse pancreatic islets, pure rat B cells or insulin-producing cells of the RINm5F line catalyzed the hydrolysis of d-glucose-6-phosphate. Relative to protein content, the enzymic activity, which was mainly associated with particulate rather than soluble subcellular material, was much lower in endocrine pancreatic cells than in liver. The rat islet enzyme differed from liver glucose-6-phosphate by its lower affinity for d-glucose-6-phosphate, its lower pH optimum, its greater relative efficiency towards l-glycerol-3-phosphate as distinct from d-glucose-6-phosphate, its restricted lability during exposure to pH 5.0, its inability to act as a glucose-6-phosphate:glucose phosphotransferase, and its insensitivity to inhibition by D-glucose. It is concluded that rat islet cells are virtually devoid of true glucose-6-phosphatase activity.
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