Purification to homogeneity of H blood group beta-galactoside alpha 1 leads to 2 fucosyltransferase from porcine submaxillary gland.

摘要: A beta-galactoside alpha 1 leads to 2 fucosyltransferase has been solubilized from porcine submaxillary glands and purified 124,000-fold homogeneity by repeated affinity chromatography on GDP-hexanolamine agarose. Sodium dodecyl sulfate polyacrylamide gel electrophoresis of the enzyme revealed two electrophoretic species with apparent Mr = 60,000 55,000. The have not completely resolved, but both appear be active forms approximately equal specific activities. Glycosidase digestion fucosylated products 2-specific fucosidase Clostridium perfringens 3/alpha 4-specific almond emulsin indicates that exclusively Fuc 2Gal linkage a variety acceptor substrates. GDP-fucose hydrolase activity co-purifies fucosyltransferase. Identical rates thermal inactivation co-migration under nondenaturing conditions suggest activities are due single species.