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Abstract
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 preparation was revealed homogeneous by polyacrylamide gel electrophoresis in the presence and absence of sodium dodecyl sulfate. There was no significant difference in thermal stabilities of the two activities. From these results it was concluded that the UDPglucose and UDPgalactose pyrophosphorylase activities in B. bifidum are catalyzed by a single enzyme protein.
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