通过亲和色谱法纯化硫代半乳糖苷转乙酰酶。

Purification of thiogalactoside transacetylase by affinity chromatography.

作者信息

Zabin I, Fowler A V

出版信息

Anal Biochem. 1984 Feb;136(2):493-6. doi: 10.1016/0003-2697(84)90250-1.

Abstract

Thiogalactoside transacetylase, the product of the lacA gene of the lactose operon of Escherichia coli, has been purified by an improved procedure. The enzyme binds tightly to immobilized Cibacron Blue F3GA columns and can be eluted by potassium chloride in high concentrations. Final purification was obtained by affinity chromatography on an agarose-coenzyme A column followed by gel filtration.

摘要

硫代半乳糖苷转乙酰酶是大肠杆菌乳糖操纵子中lacA基因的产物，已通过改进的方法进行了纯化。该酶与固定化的汽巴蓝F3GA柱紧密结合，可被高浓度的氯化钾洗脱。通过在琼脂糖-辅酶A柱上进行亲和层析，然后进行凝胶过滤，最终实现了纯化。