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Purification of poliovirus by affinity chromatography

✍ Scribed by Fred Brown; Bryan O. Underwood; Karl H. Fantes

Publisher
John Wiley and Sons
Year
1979
Tongue
English
Weight
240 KB
Volume
4
Category
Article
ISSN
0146-6615

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✦ Synopsis

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 could be re-used and its capacity was sufficiently high to make it a useful method for the purification of milligram quantities of the virus.

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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 wa