The sorbitol-oxidizing enzyme of red blood cells

The sorbitol-oxidizing enzyme of human erythrocytes has been partially purified and characterized. Its kinetic characteristics were found to be similar to the sorbitol dehydrogenase of sheep liver and the DPN-xyluloxe dehydrogenase which have been isolated from sheep liver and guinea pig liver, respectively. Although this enzyme is able to oxidize sorbitol relatively efficiently, it has very little activity toward dulcitol, and therefore cannot account for the high K-m pathway of methemoglobin reduction by galactose.