Hiraiwa M, Shiraishi T, Uda Y
J Biochem. 1986 Jul;100(1):255-8. doi: 10.1093/oxfordjournals.jbchem.a121701.
The multiplicity of bovine liver acid beta-galactosidase was investigated. Acid beta-galactosidase activity was measured in the presence of glucono-delta-lactone, which inhibited the neutral beta-galactosidase activity but not the acid beta-galactosidase activity in bovine liver. Three forms of acid beta-galactosidase were separated by Sephadex G-200 gel filtration and the elution pattern of the 4-methylumbelliferyl-beta-galactosidase activity coincided with that of the GM1-beta-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.
对牛肝酸性β-半乳糖苷酶的多样性进行了研究。在葡萄糖酸-δ-内酯存在的情况下测定酸性β-半乳糖苷酶活性，葡萄糖酸-δ-内酯可抑制牛肝中的中性β-半乳糖苷酶活性，但不抑制酸性β-半乳糖苷酶活性。通过Sephadex G-200凝胶过滤分离出三种形式的酸性β-半乳糖苷酶，4-甲基伞形酮基-β-半乳糖苷酶活性的洗脱模式与GM1-β-半乳糖苷酶活性的洗脱模式一致。这些形式在酸性条件（pH 4.5）下相对稳定，但两种高分子量形式在中性条件（pH 7.0）下倾向于解离成低分子量形式。这三种形式的酶对GM1神经节苷脂表现出相似的最适pH值和表观米氏常数。
