Abstract
Here we describe a single-step affinity column for purification of vectors based on adeno-associated virus type 5 (AAV5). A sialic-acid-rich protein called mucin was covalently attached to Sepharose and was found to bind AAV5 vectors. Elution with high salt efficiently recovered highly active vectors of greater purity than what is achieved with CsCl(2) sedimentation.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Cell Line
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Cesium
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Chlorides
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Chromatography, Affinity / methods*
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Dependovirus / classification*
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Dependovirus / isolation & purification*
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Dependovirus / metabolism
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Dependovirus / physiology
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Genetic Vectors / isolation & purification*
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Humans
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Male
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Mice
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Mice, Inbred C57BL
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Mucins / metabolism
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Muscle, Skeletal / virology
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Salts / pharmacology
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Sepharose / metabolism
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Ultracentrifugation
Substances
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Chlorides
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Mucins
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Salts
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Cesium
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Sepharose
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cesium chloride