固定于琼脂糖4B上的幼鼠脑β-半乳糖苷酶对糖脂和糖蛋白中半乳糖的水解作用。

Hydrolysis of galactose from glycolipids and glycoprotein by young rat brain beta-galactosidases immobilized to Sepharose 4B.

作者信息

Yeung K K, McKinney R A, Dain J A

出版信息

J Neurochem. 1980 Aug;35(2):407-11. doi: 10.1111/j.1471-4159.1980.tb06279.x.

DOI:10.1111/j.1471-4159.1980.tb06279.x

Abstract

An extract of glycosidic enzymes from young rat brain was immobilized to cyanogen bromide-activated Sepharose 4B. Most glycosidases retained approximately 10--25% of their activities after immobilization. Immobilized beta-galactosidases were used repeatedly without detectable loss of enzyme activity in the hydrolysis of p-nitrophenyl-beta-D-galactopyranoside. In addition to the synthetic substrate, the immobilized rat brain beta-galactosidases could also hydrolyze galactose from lactose, galactosylcerebroside, asialofetuin, and GM1-ganglioside. The hydrolysis of GM1- to GM2-ganglioside was confirmed on TLC.

摘要

将幼鼠脑内的糖苷酶提取物固定在溴化氰活化的琼脂糖凝胶4B上。大多数糖苷酶在固定后仍保留其约10 - 25%的活性。固定化的β-半乳糖苷酶可反复使用，在对硝基苯基-β-D-吡喃半乳糖苷的水解中未检测到酶活性损失。除了合成底物外，固定化的鼠脑β-半乳糖苷酶还能从乳糖、半乳糖脑苷脂、去唾液酸胎球蛋白和GM1神经节苷脂中水解半乳糖。在薄层色谱法上证实了GM1神经节苷脂向GM2神经节苷脂的水解。