Abstract
From rat liver has been purified sorbitol dehydrogenase in high purity, showing a single line by means of disc electrophoresis. The substrate specificity of the purified enzyme was very low; the Km value of the enzyme was 4.5×10-4M for sorbitol, 2.6×10-4M for xylitol and 2.4×10-3M for ribitol, respectively. The localization of sorbitol dehydrogenase was investigated by use of both fluorescein-labeled and peroxidase-labeled antibody methods on the light microscopic level. The antigen was recognized concentratedly around the nucleus and in less amount in the other parts of the cytoplasm of the liver cells in a granular profile. In the electron microscopic study by means of peroxidase-labeled antibody technique, the positive deposits were observed in the reticulated or net-like pattern in the amorphous part of the cytoplasm of parenchymal cells, which might correspond to the glycogen area. The results of the present study generally coincided with those of the foregoing report, in which the proper enzyme was demonstrated by using a histochemical technique in light and electron microscopy.
