Mild interaction of proteins with butyl and hydroxyl groups on the surface of polymer gels TSK HW-65 and butyl toyopearl 650-M.

Interaction of bovine serum albumin (BSA) with butyl and hydroxyl groups on adsorbent gel surfaces was investigated by using TSK HW-65 and Butyl Toyopearl 650-M gels. It was found that BSA was adsorbed on the gel not only from highly concentrated ammonium sulphate but also from dilute perchloric acid, trichloroacetic acid, etc. Some eluent modifiers, such as organic solvents (30% aqueous methanol or acetonitrile), salt solutions (0.18-0.2 M phosphate) and hydrogen-bond breaking reagents (3-7 M urea, 10 M ethylene glycol, 0.1% triethylamine) were found to be effective in facilitating the elution of trapped BSA from the gel. The conformational change of BSA in these solutions was slight except for urea, and it was reversibly recovered after removal of the modifier from the aqueous solutions, except for the hydrogen-bond breaking reagents.