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Purification of thiogalactoside transacetylase by affinity chromatography

✍ Scribed by Irving Zabin; Audree V. Fowler

Publisher
Elsevier Science
Year
1984
Tongue
English
Weight
309 KB
Volume
136
Category
Article
ISSN
0003-2697

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✦ Synopsis

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.

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Poliovirus type 1 (Mahoney strain) has been purified by retention on a Sepharose 4B-antibody column and elution with 3M K thiocyanate. The virus was recovered in excellent yield and its purity was as high as that achieved by detergent treatment followed by sucrose gradient centrifugation. The column