MEASUREMENT OF KINETIC BINDING CONSTANTS OF VIRAL ANTIBODIES USING A NEW BIOSENSOR TECHNOLOGY

Association (k(a)) and dissociation (k(d)) rate constants of three monoclonal antibodies raised against tobacco mosaic virus were determined using a biosensor technique based on surface plasmon resonance (BIAcore, Pharmacia). Dissociation rates were constant over the 4-400 nM antibody concentration range whereas apparent association rates decreased over this range probably due to an increased saturation level of the antigen. Affinity constants K calculated from the ratio of k(a)/k(d) were in reasonable agreement with values obtained under equilibrium conditions by two standard methods based on enzyme immunoassay.