Tatsurokuro Tochikura

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An enzyme having both UDP-glucose (UDP-Glc) and UDP-galactose (UDP-Gal) pyrophosphorylase activities was purified to homogeneity from Bifidobacterium bifidum. The molecular weight of the enzyme was about 200,000 and it appeared to be composed of four identical subunits. The purified enzyme showed almost the same reactivity towards UDP-Glc and UDP-Gal, and(More)
Wepreviously reported the purification and the characterization of an endo-a-GalNAc-ase found in the culture fluid of Alcaligenes sp. isolated from soil.7 8) This enzyme was found to release a disaccharide (galactose /H ->3 Nacetylgalactosamine) from a wide variety of glycoproteins and glycopeptides containing O-linked oligosaccharides.8) As this(More)
The enzyme preparation catalyzing the pyrophosphorolyses of UDP-glucose and UDPgalactose almost at the same rate was purified about 900-fold from Bifidobacterium bifidum grown on glucose medium. The two activities were always associated with each other, and their activity ratio was always constant throughout the purification steps. The final preparations(More)
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