The heterogeneity and acceptor specificity of human serum galactosyltransferase.

Human serum was fractionated by high resolution agarose isoelectricfocusing and the galactosyltransferase activity profile was determined using the ovalbumin, mucin, glucose and N-acetylglucosamine acceptor assays. The four acceptors gave very similar activity profiles. There were minor quantitative differences in some of the 12 or more peaks of activity detected and the only qualitative difference between them was a minor peak at pH 3.90 (2% of the total activity) which reacted only with the mucin acceptor. This suggests that most of the isoenzymes of human serum galactosyltransferase have broad and similar acceptor specificities and that the heterogeneity seen in serum cannot be accounted for by acceptor-specific forms of the enzyme.