In Golgi-enriched membrane fraction isolated from alloxan diabetic rat liver, the protein content is lower but the protein composition is similar to normal. The specific activity of galactosyl transferase in this membrane fraction is higher than normal, but the total activity of the enzyme in the whole liver is normal. Great dispersion is found among the individual values. Differences in the specific activities of some other marker enzymes were also found in the Golgi-enriched membrane fraction. The morphology of the Golgi complex examined in either thin sections of Golgi-enriched fraction or ultra-thin sections of livers appears normal. A slight reduction of the rough endoplasmic reticulum is observed. The results obtained are discussed in comparison with those obtained for streptozotocin diabetic rat liver.