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Abstract
A Golgi apparatus-rich fraction isolated from rat liver catalyzed the transfer of galactose from UDP-galactose to N-acetylglucosamine with the formation of N-acetylaminolactose as well as the transfer of glucosamine from UDP-N-acetyl- glucosamine to endogenous protein acceptors. Based on enzymatic and morphological criteria, Golgi apparatus fractions were estimated to contain at least 80% Golgi apparatus-derived material. Approximately half of the total glycosyl transferase activities of the original homogenates was recovered in the Golgi apparatus fraction. The glycosyl transferase activities of purified endoplasmic reticulum fractions were much lower than those of the Golgi apparatus. Plasma membrane fractions as well as the soluble supernatant fraction contained little or no activity.
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