PubMed:6425294 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PubMed/sourceid/6425294","sourcedb":"PubMed","sourceid":"6425294","source_url":"http://www.ncbi.nlm.nih.gov/pubmed/6425294","text":"Purification and characterization of UDP-N-acetylgalactosamine: globotriaosylceramide beta-3-N-acetylgalactosaminyltransferase, a synthase of human blood group P antigen, from canine spleen.\nA UDP-N-acetylgalactosamine:globotriaosylceramide beta-3-N-acetylgalactosaminyltransferase which catalyzes the conversion of human blood group Pk antigen into P antigen has been purified over 18,000-fold in 4% yield from a Triton X-100 extract of canine spleen microsomes by affinity chromatography on UDP-hexanolamine-Sepharose and globotriaosylceramide acid-Sepharose. The purified enzyme migrates as two major bands with apparent molecular weights of 64,000 and 57,000 on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. A single band, with enzyme activity, was observed in nondenaturing acrylamide gels containing Triton X-100. Mn2+ was required for activity, and the pH optimum was 6.9. Km values for UDP-GalNAc and globotriaosylceramide were 14 and 2.5 microM, respectively. Studies on substrate specificities indicate that the preferred substrates have the general structure Gal alpha 1-4Gal-OR in which the nature of the R moiety has relatively little effect on activity. An antibody against the purified enzyme eliminated the activity of the enzyme, but did not neutralize the alpha-3-N-acetylgalactosaminyltransferase involved in the biosynthesis of Forssman 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