Residual activity of alpha-galactosidase A in Fabry's disease.
The alpha-galactosidase A activity from fibroblasts of five Fabry patients and five controls has been separated from alpha-galactosidase B through small DEAE-cellulose columns and in some experiments by treatment of the fibroblast extracts with Sepharose coupled to anti-alpha-galactosidase B antibodies. By these independent methods, it has been shown that there is a residual alpha-galactosidase A in Fabry's disease, which is immunologically similar to the alpha-galactosidase A from the controls. The alpha-galactosidase A from all of the patients and controls has the same apparent Km value for the synthetic substrate 4-methylumbelliferyl-alpha-galactosidase A, while the fifth has a thermolabile enzyme like that from the controls. The amount of immunologically active alpha-galactosidase A seems to be decreased in the patients tested.
D001666:Binding Sites, Antibody; D000795:Fabry Disease / Q000201:enzymology*; D005347:Fibroblasts / Q000201:enzymology; D005696:Galactosidases / Q000276:immunology / Q000378:metabolism*; D002517:Galactosylgalactosylglucosylceramidase / Q000378:metabolism; D006801:Humans; D007700:Kinetics; D013696:Temperature
D005696:Galactosidases; D002517:Galactosylgalactosylglucosylceramidase