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- W2019925350 abstract "A UDP-N-acetylgalactosamine: ganglioside GM3β-N-acetylgalactosaminyltransferase which catalyzes the conversion of ganglioside GM3 to GM2 has been purified over 6300-fold from a Triton X-100 extract of rat liver particulate fractions by hydrophobic chromatography and affinity chromatography on GM3-acid-Sepharose. The purified enzyme has two identical subunits of 64 000 daltons. The enzyme has a pH optimum of pH 6.7–6.9 and requires divalent cations such as Mn2+ and Ni2+. In studies on substrate specificity GM3 containing N-acetylneuraminic acid (GM3(NeuAc)) and GM3 containing N-glycolylneuraminic acid were both good acceptors for the purified enzyme. The plots of the activity of transferase as a function of GM3(NeuAc) showed sigmoidal relationships. The oligosaccharide of GM3, sialyllactose, was also a good acceptor, which indicates that the preferred acceptor substrate has the possible structure NeuAcα2- or NeuGcα2-3 Galβ1-4Glc-OR." @default.
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- W2019925350 date "1987-06-01" @default.
- W2019925350 modified "2023-10-02" @default.
- W2019925350 title "Purification and properties of GM2 synthase, UDP-N-acetylgalactosamine: GM3β-N-acetylgalactosaminyltransferase from rat liver" @default.
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- W2019925350 doi "https://doi.org/10.1016/0005-2760(87)90260-8" @default.
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