Abstract
Extract: Several properties of β-galactosidase obtained from brains of controls and patients with Gm1 gangliosidosis types I and II were studied. The pH optimum of β-galactosidase was 4 in both fetal and control brain. In contrast, the pH optimum of brain β-galactosidase in patients with either type I or type II Gm1 gangliosidosis was 3. The residual β-galactosidase activity in brains of both type I and type II patients was approximately 27% and 6% of the control values when assayed at pH 3 and 4, respectively. Differences in the thermostability of β-galactosidase in control, type I, and type II patients were observed.
On both cellulose acetate and starch gel electrophoresis, brains from type I patients, but not from type II patients had a β-galactosidase band which migrated towards the anode with a mobility different from that in control brains.
Speculation: The two clinical phenotypes of Gm1 gangliosidosis are determined by mutational events which occur either at different loci of a gene or at different genes. In addition, both disorders appear to be the result of structural gene mutations.
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Chou, L., Kaye, C. & Nadler, H. Brain β-Galactosidase and Gm1 Gangliosidosis. Pediatr Res 8, 120–125 (1974). https://doi.org/10.1203/00006450-197402000-00009
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DOI: https://doi.org/10.1203/00006450-197402000-00009
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