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Membranes of Mammary Gland. IX. Concentration of Glycosphingolipid Galatosyl and Sialytransferases in Golgi Apparatus from Bovine Mammary Gland

Department of Animal Sciences, Purdue University, Lafayette, Indiana 47907

ABSTRACT

Glycosyl transferases catalyzing the transfer of galactose from UDP-galactose to glucosyl ceramide and N-acetylnuer-aminic acid from CMP-N-acetylneur-aminic acid to lactosyl ceramide were enriched 10 to 15 times in Golgi apparatus relative to total particulate fractions. These transferase activities were low in rough endoplasmic reticulum and were absent from the plasma membrane-derived milk fat globule membrane. Sialyl transferases utilizing N-acetylneur-aminylgalactosylglucosylceramide and galactosyl - N - acetylgalactosaminyl - (N - ace-tylneuraminy 1) -galactosylglucosylcera-mide as acceptors were also present in high specific activity in Golgi apparatus fractions. These results demonstrate that the neutral glycolipids and gangliosides of milk are glycosylated at the level of Golgi apparatus in the mammary epithelial cell.