Abstract
Galactosemia, a recessively inherited disorder, is caused by a deficiency of galactose-l-phosphate uridyl transferase (transferase). Variants of transferase which are not associated with classical galactosemia have been described. A patient with the classical clinical manifestations of galactosemia has been stuided and was shown to have one-third of normal transferase activity in festations of galactosemia has been studied and was shown to have one-third of norma; transferase acitivity in heparinized blood. Tansferase of this patient is highly unstable and no activity could be detected after 72 h of storage in heparin wheras normal enzyme is stable for months. Transferase activity of the patient's red blood cells immediately falls to zero upon exposure to isotonic phosphate buffer, pH 7.4. Transferase activity in heparinized blood from both parents is approximately three-quarters of normal and exposure of their red blood cells to isotonic phosphate buffer results in 50% inhibition. Starch gel electrophoresis of hemolysates from the patient had no detectable activity while hemolysates of the mother and maternal grandmother have shown a decreased mobility as compared to normal.
These data are interpreted as evidence for a new variant of ‘classical’ clinical galactosemia. The presence of transferase activity in patients with clinical manifestations of galactosemia may not exclude the diagnosis of this condition and may in fact represent a generalized phenomenon applicable to many familial metabolic disorders.
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Chacko, C., Christian, J. & Nadler, H. Unstable Galactose-1-phosphate Uridyl Transferase: A New Variant of Galactosemia. Pediatr Res 4, 439 (1970). https://doi.org/10.1203/00006450-197009000-00023
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DOI: https://doi.org/10.1203/00006450-197009000-00023