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2003 | 104 | 3-4 | 321-326
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Force Spectroscopy of Polyclonal and Monoclonal Anti-Bovine Serum Albumin Antibodies - BSA Complexes

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The specific interactions between bovine serum albumin and poly- or two monoclonal bovine serum albumin antibodies were studied using force spectroscopy mode of atomic force microscopy. The histograms of the unbinding forces for polyclonal bovine serum albumin antibodies are broad at high antibody concentrations (50 or 270 μg/ml) and narrow at low concentrations (10 or 27 μg/ml), while the histograms for monoclonal antibodies peak at well defined unbinding force. The peak unbinding force depends on the type of antibody and the antibody concentration. In this paper we described and characterized the passive adsorption and covalent immobilization of proteins for tip and sample preparation. Force spectroscopy could serve as a useful method for characterization of antigen-antibody interactions for measuring the specificity of an antibody or to assess the purity of a monoclonal antibody solution and to distinguish between different antibodies.
  • Institut de Physique de la Matière Condensée, University of Lausanne, 1015 Lausanne, Switzerland
  • Institut de Physique de la Matière Condensée, University of Lausanne, 1015 Lausanne, Switzerland
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