抄録
The multiplicity of bovine liver acid β-galactosidase was investigated. Acid β-galactosidase activity was measured in the presence of glucono-δ-lactone, which inhibited the neutral β-galactosidase activity but not the acid β-galactosidase activity in bovine liver. Three forms of acid, β-galactosidase were separated by Sephadex G-200 gel filtration and the elution pattern of the 4-methylumbelliferyl-β-galactosidase activity coincided with that of the GMl-β-galactosidase activity. These forms were relatively stable under acidic conditions (pH 4.5), but the two high molecular weight forms were inclined to dissociate into the low molecular weight form under neutral conditions (pH 7.0). The three forms of the enzyme showed similar pH-optima and apparent Michaelis constants for GM1 ganglioside.
