Solubilization of murine melanoma xylosyltransferase and galactosyltransferase activities and their inactivation by dialdehyde nucleosides.

The enzymes involved in the initial steps in the biosynthesis of glycosaminoglycans were examined in the murine B16 melanoma. Approximately 60% of the melanoma xylosyltransferase activity and nearly all of the galactosyltransferase activity were membrane-bound; these enzymatic activities were solubilized by treatment with Nonidet P-40 and potassium chloride, and the Michaelis constants for the substrates and acceptor molecules were determined and found to be comparable to those reported for these enzymes from the chick embryo and a rat chondrosarcoma. Dialdehyde nucleosides, which have been reported to alter the activity of several enzymes involved in nucleic acid synthesis, inhibited both xylosyltransferase and galactosyltransferase activities, with galactosyltransferase being considerably less sensitive than xylosyltransferase. The inhibition of xylosyltransferase by dialdehyde nucleosides was irreversible, with no apparent specificity for the base moiety of the dialdehyde nucleosides.