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Biosynthesis of a Globoside-type Glycosphingolipid by a -N-Acetylgalactosaminyltransferase from Embryonic Chicken Brain

From the ¹ From the Department of Chemistry, Biochemistry and Biophysics Program, University of Notre Dame, Notre Dame, Indiana 46556

A -N-acetylgalactosaminyltransferase activity has been detected in 11-day-old embryonic chicken brain which catalyzes the transfer of N-acetylgalactosamine from UDP-N-acetyl[¹⁴C]galactosamine to a triglycosylceramide (or, GloboTri-cer; O--galactosyl(14)-O--galactosyl(14)-O- -glucosyl(11)-ceramide) to form the globoside-type tetraglycosylceramide, GalNAc Gal Gal Glc ceramide. The enzyme is membrane bound and requires sodium taurocholate and Mn²⁺ for optimal activity. The optimum pH value for the incorporation of N-acetylgalactosamine was 6.5 in 2-(N-morpholino)ethanesulfonic acid buffer. The K_m values were 1.7 x 10^-3 m and 2.0 x 10^-4 m for GloboTri-cer and UDP-GalNAc, respectively. The radioactive product of the reaction was isolated, purified, and characterized as globoside-type tetraglycosylceramide. The terminal [¹⁴C]GalNAc was cleaved 78% by the action of jack bean -N-acetylgalactosaminidase. The ¹⁴C product formed a precipitin line with anti-globoside serum, and the line fused with that of globoside derived from porcine heart or erythrocytes.

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