title: Measurement of kinetic binding constants of viral antibodies using a new biosensor technology.
abstract: Association (ka) and dissociation (kd) 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 ka/kd were in reasonable agreement with values obtained under equilibrium conditions by two standard methods based on enzyme immunoassay.
authors.affiliation: Laboratoire d'Immunochimie, UPR 9021, CNRS, Institut de Biologie Moléculaire et Cellulaire, Strasbourg, France.
authors.forename: J L
authors.initials: JL
authors.lastname: Pellequer
authors.forename: M H
authors.initials: MH
authors.lastname: Van Regenmortel
mesh_terms: D000911:Antibodies, Monoclonal / Q000378:metabolism; D000914:Antibodies, Viral / Q000378:metabolism*; D015374:Biosensing Techniques; D005069:Evaluation Studies as Topic; D007124:Immunoenzyme Techniques; D007158:Immunologic Techniques; D007700:Kinetics; D014027:Tobacco Mosaic Virus / Q000276:immunology
chemical_list: D000911:Antibodies, Monoclonal; D000914:Antibodies, Viral