Abstract
Composite anion exchangers for chromatography of proteins were prepared by chemical adsorption of poly( p-nitrophenyl acrylate) on γ-aminopropylsilicas followed by coupling of the esters to 2-diethylaminoethylamine. Separation of standard proteins (bovine serum albumin and ovalbumin) on these anion exchangers established their enhanced selectivity and milder desorption conditions as compared with polyethyleneiminesilicas and DEAE-Toyopearl 650M. Frontal analysis was used to evaluate the maximum binding capacity for ovalbumin adsorption on the new packing, which was found to be 13 mg/ml and so nearly half those observed with polyethyleneiminesilicas of comparable pore diameter. The possible role of the excluded volume of the attached polymer is discussed with respect to the adsorptivity of the composite ion exchangers.
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