Biochemical studies of a human low-activity galactose-1-phosphate uridyl transferase variant.
J Inherit Metab Dis, 1978;1(4):145-51.
Ng WG, Kline F, Lin J, Koch R, Donnell GN
PMID: 117249
Impact factor: 4.75
Abstract
A low activity galactose-1-phosphate uridyl transferase (transferase) variant in a newborn infant has been demonstrated by biochemical studies in erythrocytes and cultured skin fibroblasts. The newborn infant was a galactosaemic suspect identified in a neonatal metabolic screening programme. On breast feeding, he did well without clinical symptoms of galactosaemia during the first 15 days of life. However, substantial amounts of erythrocyte galactose-1-phosphate and urinary galactitol corresponding to the levels in untreated galactosaemic patients, along with mild amino aciduria, were found. The transferase activity, as measured by a sensitive micro kinetic radioisotopic method, was about 7--10% of the normal. On starch gel electrophoresis, the enzyme from the haemolysate had similar mobility as the normal in Tris--glycine buffer, pH 8.8 and phosphate buffer, pH 7.0, but had a slower mobility than that of the normal in the histidine buffer, pH 7.8. The mobility difference was much clearer in a semipurified enzyme preparation. The transferase enzyme in the haemolysate appeared to be more heat labile.
MeSH terms
Cells, Cultured; Electrophoresis, Starch Gel; Erythrocytes; Fibroblasts; Galactosemias; Genetic Variation; Humans; Infant, Newborn; Kinetics; Male; Nucleotidyltransferases; Skin; UDPglucose-Hexose-1-Phosphate Uridylyltransferase
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