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Preparation of a stable folate-Sepharose complex for affinity chromatography

✍ Scribed by Craig Fischer; Sheldon P. Rothenberg; Maria da Costa

Publisher: Elsevier Science
Year: 1978
Tongue: English
Weight: 283 KB
Volume: 85
Category: Article
ISSN: 0003-2697
DOI: 10.1016/0003-2697(78)90267-1

No coin nor oath required. For personal study only.

✦ Synopsis

A st&le folk acid aEinity gel has been developed for the puritication of nanogmms of protein that bind folic acid or its derivatives. The affinity gel was prepared by Ant coupling folk. acid covalently to bovine serum albumin, followed by covalent coupling of the albumin to p-benzoquinone-activated

Sephaiuse. Mer the albumin-folk acid complex was formed, it was treated with charcoal to remove ionicalty bound folate which would otherwise elute from the gel and decmase the recovery of the binding protein. Thep-benzoquinone activation resulted in a more stable binding of the albumin to the Sepharose.

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