Abstract
Fibroblasta from a patient with Fabry's disease have an α-galactosidase activity corresponding to 10–20% of control values, and the same difference has been found between the 2 clonal populations derived from the patient's mother and sister (Science 170: 180, 1970). The α-galactosidase present in fibroblasta of 2 unrelated patients and in “negative” clones of 2 heterozygotes shows a slower rate of heat inactivation than the enzyme of “positive” clones and controls. The α-galactosidase from uncloned fibroblasts of a heterozygote shows a rate of inactivation indicative of a mixture of 2 enzymes. Moreover a small reproducible difference in the apparent Km value between the wild-type and the mutant enzyme from one patient adds evidence for the structural character of this mutation. The specific activity of both mutant and wild-type α-galactosidase increases 10 and 4 times respectively, if the fibroblasts are maintained in a stationary phase of growth, while the activity of β-galactosidase increases fivefold in normal and α-galactosidase deficient cells. This has made possible electrophoretic analysis of the mutant α-galactosidase which, in the one family examined, does not migrate differently from the wild-type enzyme on Cellogel at pH 5.0.
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Romeo, G., Migeon, B. Fabryl's disease: Evidence for structural mutation of α-galactosidase. Pediatr Res 5, 420–421 (1971). https://doi.org/10.1203/00006450-197108000-00207
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DOI: https://doi.org/10.1203/00006450-197108000-00207