Abstract
Acid beta-galactosidase activity can be separated into multiple molecular forms by isoelectric focusing on cellulose acetate membranes. The residual acid beta-galactosidase in the juvenile form of GM1 gangliosidosis has three bands of enzyme activity with an apparent isoelectric pH (pI) range from 4.9 to 5.2, whereas that in the infantile form has a single band with an apparent pI of 5.2. Separation of residual acid beta-galactosidase into multiple molecular forms by analytical isoelectric focusing demonstrates enzymatic differences that can be correlated with the allelic mutations that affect the GM1 ganglioside beta-galactosidase locus.
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