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  • Title: Enzymatic characterization of UDP-galactose:FdSdG galactosyltransferase in purified liver plasma membrane.
    Author: Fernandez-Briera A, Louisot P, Morelis R.
    Journal: Biochem Int; 1989 Feb; 18(2):415-28. PubMed ID: 2504163.
    Abstract:
    This study yields evidence for the localization of a galactosyltransferase in purified liver plasma membranes, with the following results. The purified plasma membranes contained galactosyltransferases which transfered galactose from UDP-galactose into desialylated-degalactosylated fetuine. A suitable system of glycosylation reaction was defined. It contained: 10 mM Tris-HCl pH 7.4, 5 mM Mn2+, 4 mM NaF. For the assay with exogenous acceptors, 1.6 mg/ml of desialylated-degalactosylated fetuine and 0.1% of triton X-100 were added. The apparent Km values for UDP-galactose were about 10(-5) M. Enzymatic activities required Mn2+. This cation appeared to be a linear non-competitive activator when used at concentrations below 5 mM. Mg2+ and Ca2+ had an inhibitory effect on Mn2+-dependant-galactosyltransferase.
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