Abstract
UDP-Gal pyrophosphorylase (UTP:α- d-galactose-1-phosphate uridyltransferase, EC 2.7.7.10) and UDP-Glc pyrophosphorylase (UTP:α- d-glucose-1-phosphate uridyltransferase, EC 2.7.7.9) activities have been detected in cultivated human skin fibroblasts and their properties compared. UDP-Glc pyrophosphorylase is more stable at 50 and 56° than UDP-Gal pyrophosphorylase while both enzymes have similar K m values, pH optima and electrophoretic mobility. On the basis of the difference in thermal stability, it has been suggested that UDP-Gal pyrophosphorylase is an enzyme distinct from UDP-Glc pyrophosphorylase. A possible alternate pathway for the metabolism of galactose in the galactosemic individuals is discussed.
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