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Glycosyltransferase activities were measured in normal monocytes and in leukaemic monoblasts. Biosynthesis of glycosylated derivatives of dolichyl-monophosphate, which act as intermediates in glycosylation, was measured. Transfer of mannose from GDP-mannose was greatly increased in leukaemic monoblasts. Galactosyltransferase activities, using endogenous protein acceptors, were increased in leukaemic cells of the monocytic lineage compared to normal cells. No significant difference was observed on specific exogenous glycoprotein acceptors. These selective increases of some glycosyltransferase activities in normal and leukaemic monocytic cells can be correlated either with different expression of specific carbohydrate structures or with changes in glycosylation regulation.
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