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Updated: Jul 28, 2026

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Identification of protein complexes with quantitative proteomics in S. cerevisiae
Published on: March 4, 2009
Purification of thiogalactoside transacetylase by affinity chromatography
Analytical Biochemistry
|February 1, 1984
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.

