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  • Title: Immunoaffinity chromatography utilizing monoclonal antibodies. Factors which influence antigen-binding capacity.
    Author: Pfeiffer NE, Wylie DE, Schuster SM.
    Journal: J Immunol Methods; 1987 Feb 26; 97(1):1-9. PubMed ID: 2880913.
    Abstract:
    Differences in antigen-binding capacity of a monoclonal antibody coupled to Sepharose under varying conditions were explored. The extent of cyanogen bromide activation, and the pH of the coupling reaction had a profound effect upon the rate of antibody coupling, but only small differences in antigen-binding capacity were observed if the antibody coupling reaction was terminated when 80-90% of the antibody was covalently coupled to Sepharose. However, if antibody was incubated with activated resin until 100% coupling was attained, the antigen-binding capacity of the resulting immunoadsorbent decreased significantly. Monoclonal antibody coupled to Sepharose via an N-hydroxysuccinimide ester linkage and approximately half the antigen-binding capacity of antibody coupled by CNBr activation. Concentrations of monoclonal antibodies as high as 13 mg/ml of packed resin could be used without noticeable steric hindrance.
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