Galactose 1-phosphate uridylyltransferase was partially purified from red blood cells of six different galactosemic patients. Cross-reacting material in these preparations, demonstrated by double immunodiffusion with an antiserum to normal human enzyme, not only lacks catalytic activity for the interconversion of the natural substrates, UDP-glucose + galactose-1-P ⇌ UDP-galactose + glucose-1-P, but also fails to catalyze the exchange of radioisotope in either of the two half-reactions of the double displacement sequence by which activity is expressed.
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Wu et al. (1974) studied this question.
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