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  • Title: Purification and characterization of human serum galactosyltransferase (lactose synthetase A protein).
    Author: Fujita-Yamaguchi Y, Yoshida A.
    Journal: J Biol Chem; 1981 Mar 25; 256(6):2701-6. PubMed ID: 6782094.
    Abstract:
    A galactosyltransferase, which transfers galactose from UDP-galactose to N-acetylglucosamine, was purified 286,000-fold to homogeneity with 40% yield from human plasma by repeated affinity chromatography on alpha-lactalbumin-Sepharose. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the purified enzyme showed a single protein band with molecular weight of 49,000. The enzyme is a glycoprotein with 11% by weight carbohydrate, which seems to have only asparagine-N-acetylglucosamine linkage-type carbohydrate chains. The enzyme showed characteristic changes in activity at different alpha-lactalbumin concentrations, indicating that the enzyme is the A protein of lactose synthetase. Km values for the substrates were found to be 0.056 mM for UDP-galactose, 3.2 mM for GlcNAc, and 0.44 mM for Mn2+, and in the presence of alpha-lactalbumin, 3.4 mM for Glc, and 0.20 mM for Mn2+. The activity of the enzyme was neutralized by anti-enzyme antibody, but the antibody did not neutralize the bovine milk galactosyltransferase (A protein) activity.
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