A prevalent mutation for galactosemia among black Americans.

OBJECTIVE  To define the mutation causing galactosemia in patients of black American origin who have no galactose-1-phosphate uridyltransferase (GALT) activity in erythrocytes but good clinical outcome.
METHODS  We discovered a mutation caused by a C-- > T transition at base-pair 1158 of the GALT gene that results in a serine-to-leucine substitution at codon 135 (S135L). We developed a method with which to screen populations for its prevalence.
We compared galactose-1-phosphate uridyltransferase among erythrocytes, leukocytes, and transformed lymphoblasts, as well as total body oxidation of D- (13C) -galactose to 13CO2 among three genotypes for GALT (S135L/S135L, Q188R/Q188R, and Normal/Normal). RESULTS  We found a 48% prevalence of the S135L mutation among 17 black American patients with classic galactosemia and a 1% prevalence in a population of 50 black Americans without galactosemia.
The S135L mutation was not found in 84 white patients with G/G galactosemia nor in 87 white control subjects without galactosemia.
We found normal whole body oxidation of D- (13C) -galactose by the patient homozygous for S135L and various degrees of enzyme impairment among different tissues.
CONCLUSIONS  The S135L mutation in the GALT gene is a prevalent cause of galactosemia among black patients.
Because GALT activity varies in different tissues of patients homozygous for S135L, they may have a better clinical outcome than patients who are homozygous for Q188R when both are treated from infancy.. 
