Galactose-1-phosphate uridyl transferase activity has been demonstrated in hybrid cells formed from the fusion of human diploid fibroblasts obtained from different patients with galactosemia.
A baby presented on day 5 with symptoms of classical galactosaemia which are believed to be owing to a lack of uridine diphosphate-4-epimerase, rather than to the usual galactose-1-phosphate uridyl transferase defect.
The most frequent cause for an abnormal result during screening of newborn infants for galactosemia is double heterozygosity for Duarte variant and galactosemia, in which galactose-1-phosphate uridyl transferase activity is reduced to approximately 17% of normal.
Galactosemia is a disorder caused by a deficiency of any one of three possible enzymes involved in the metabolism of galactose: galactokinase, transferase or epimerase.
Galactose-1-phosphate uridyl transferase (GALT), the deficient enzyme in classical galactosemia, was studied by Percoll-gradient age-fractionation of erythrocytes.
Only 12 of the 43 patients with an abnormal fluorometric screening test were found to have less than 3% GALT activity by quantitative assay, no GALT-staining by IEF, and a clinical history consistent with classical galactosemia.
Molecular characterization of two galactosemia mutations: correlation of mutations with highly conserved domains in galactose-1-phosphate uridyl transferase.
Molecular characterization of two galactosemia mutations: correlation of mutations with highly conserved domains in galactose-1-phosphate uridyl transferase.
Molecular characterization of two galactosemia mutations: correlation of mutations with highly conserved domains in galactose-1-phosphate uridyl transferase.
Molecular characterization of two galactosemia mutations: correlation of mutations with highly conserved domains in galactose-1-phosphate uridyl transferase.
Molecular characterization of two galactosemia mutations: correlation of mutations with highly conserved domains in galactose-1-phosphate uridyl transferase.
Molecular characterization of two galactosemia mutations and one polymorphism: implications for structure-function analysis of human galactose-1-phosphate uridyltransferase.
Molecular characterization of two galactosemia mutations and one polymorphism: implications for structure-function analysis of human galactose-1-phosphate uridyltransferase.
Molecular characterization of two galactosemia mutations and one polymorphism: implications for structure-function analysis of human galactose-1-phosphate uridyltransferase.
The results reported here establish the utility of the yeast-based expression system for human GALT and set the stage for more detailed studies of this important enzyme and its role in galactosemia.