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Department of Animal Sciences, Purdue University, Lafayette, Indiana 47907
ABSTRACT
Milk fat globule membranes contained glycosidase activity capable of hydrolyzing uridine diphosphogalactose and uridine diphosphoglucose with nearly equal facility. The activity was stimulated by Triton X-100 and by Mg++ but was inhibited by Hg++ and Ca++. With uridine diphosphoglucose as substrate the enzyme displayed a pH optimum of 10.0 and a Km of .5 mM. The fat globule membrane lacked activity in galactosyl transferases capable of utilizing glucose, N-acetylglucosamine, or endogenous protein as acceptors.
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