Abstract
The oxidation of D-sorbitol in rat-liver slices and homogenates is catalysed by a dehydrogenase using coenzyme I. The product of its oxidation by the partially purified dehydrogenase is D-fructose. The dehydrogenase also oxidizes L-iditol; probably to L-sorbose. The main product of the oxidation of sorbitol by liver slices is glucose. Very small quantities of fructose are also formed. Oxidation of L-iditol by slices produces small amts. of glucose and sorbose. Sorbitol and iditol considerably lower the spontaneous ketogenesis of liver slices from fasted rats. The oxidation of sorbitol to fructose by coenzyme I is reversible; as is also the oxidation of L-iditol to L-sorbose. The equilibrium constant of the former reaction is 0.240 [plus or minus] 0.013. Optimum conditions for the oxidation of sorbitol by the liver dehydrogenase are pH 7.9-8.1 and 38-40[degree]. Km = 7 x 10-4[image]. Sorbitol dehydrogenase is found in the rat only in liver and kidney. It appears to be widely distributed in mammalian liver.