Abstract
An enzyme which catalyzes the transfer of galactose from UDP-galactose to galNAc-gal-glc-ceramide is described. The enzyme is found mainly in the nervous tissue of tadpole (Taylor and Kollros stage 17), adult frog, adult and 8 day old rat. The enzymic activity is localized in the 11,500 xg, 20,000 xg and 100,000 xg particles. The UDP-galactose: galNAc-gal-glc-ceramide from the particles by treatment with sodium desoxylcholate and Triton X-100. The pH optimum for the solubilized enyme is between 6.8 and 7.0 in cacodylate buffer, and the Km is 4.25 ×10−5 M. The enzymic reaction is proportional to time for 4 hr and to the amount of protein added. The product of the transferase reaction, using galNAc-gal-glc-ceramide. A pathway for the biosynthesis of brain gangliosides requiring UDP-galactose: galNAc-gal-glc-ceramide galactosyl transferase is proposed.
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Previous publications under the name of Morris G. S. Mark.
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Yip, M.C.M., Dain, J.A. The enzymic synthesis of ganglioside: I. Brain uridine diphopphate D-galactose: N-acetyl-galactosaminyl-galactosyl-glucosyl-ceramide galactosyl transferase. Lipids 4, 270–277 (1969). https://doi.org/10.1007/BF02533185
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DOI: https://doi.org/10.1007/BF02533185