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Laboratory of Clinical Biochemistry, Mother and Child Institute, Warszawa, Poland.
Direct chromatographic isolation of UDP galactose and galactose-1-phosphate was used for determination of the activity of UDP galactose pyrophosphorylase in erythrocytes. The activity was determined by measuring the amount of UDP galactose produced from galactose-1-phosphate and uridine triphosphate. In homozygotes with galactosaemia the activity of the enzyme was nearly ten times lower than in controls, so this difference was highly significant statistically (p less than or equal to 0.001) and the respective values were 0.0051 +/- 0.0003 and 0.0418 +/- 0.0038 mumol of UDP galactose formed during 1 hour by 1 ml of erythrocytes (300 mg of haemoglobin). In heterozygotes with galactosaemia the activity of the enzyme had intermediate values between those in homozygotes and healthy controls.
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