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J. Biol. Chem., Vol. 259, Issue 13, 8045-8047, 07, 1984

Two distinct UDP-galactose: 2-acetamido-2-deoxy-D-glucose 4 beta- galactosyltransferases in porcine trachea

BT Sheares and DM Carlson

In previous studies on glycosyltransferase activities in porcine trachea, we demonstrated the presence of two galactosyltransferases which transfer galactose from UDP-galactose to N-acetylglucosamine (Sheares, B.T. and Carlson, D.M. (1983) J. Biol. Chem. 258, 9893-9898). One enzyme, UDP-galactose:N-acetylglucosamine 3 beta- galactosyltransferase, synthesized galactosyl-beta 1,3-N- acetylglucosamine while the other, UDP-galactose:N-acetylglucosamine 4 beta-galactosyltransferase, synthesized galactosyl-beta 1,4-N- acetylglucosamine. A third galactosyltransferase has now been demonstrated utilizing a solubilized membrane preparation from pig trachea, which also synthesizes galactosyl-beta 1,4-N-acetylglucosamine as determined by gas-liquid chromatography and Diplococcus pneumoniae beta-galactosidase treatment. This new UDP-galactose:N- acetylglucosamine 4 beta-galactosyltransferase is distinct from the lactose synthetase A protein in that it does not bind to alpha- lactalbumin-agarose or to N-acetylglucosamine-agarose. The enzyme is separable from the UDP-galactose:N-acetylgalactosaminyl-mucin 3 beta- galactosyltransferase by affinity chromatography on asialo ovine submaxillary mucin adsorbed to DEAE-Sephacel. This newly discovered 4 beta-galactosyltransferase binds to UDP-hexanolamine-Sepharose and is partially separated from UDP-galactose:N-acetylglucosamine 3 beta- galactosyltransferase by Sephacryl S-200 gel filtration chromatography. Neither high concentrations of N-acetylglucosamine (200 mM) nor alpha- lactalbumin inhibits the incorporation of galactose into galactosyl- beta 1,4-N-acetylglucosamine by this enzyme.
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