Galactose-1-phosphate uridyl transferase in fibroblasts: isozymes in normal and variant states.
Electorphoretic properties of galactose-1-phosphate uridyl transferase in cultured skin fibroblasts of normal humans and individuals with different enzyme variants have been studied. Normal fibroblast lysates showed four activity bands, each slower moving than the erythrocyte enzyme. The transferase variants revealed different mobilities analogous to those found in erythrocytes. These findings suggest that subunits of human transferase associate variously with one another in a manner specific for each tissue and that in transferase variant states, an altered subunit results in a characteristic alteration in electrophoretic mobility which is analogous for each tissue.
D004592:Electrophoresis, Starch Gel; D005347:Fibroblasts / Q000201:enzymology; D005690:Galactose / Q000378:metabolism; D005693:Galactosemias / Q000235:genetics*; D014644:Genetic Variation; D006801:Humans; D009713:Nucleotidyltransferases / Q000235:genetics*; D012867:Skin / Q000201:enzymology; D005694:UTP-Hexose-1-Phosphate Uridylyltransferase / Q000235:genetics*
D009713:Nucleotidyltransferases; D005694:UTP-Hexose-1-Phosphate Uridylyltransferase; D005690:Galactose