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Real Time Analysis of Antibody‐Antigen Reaction Kinetics
Author(s) -
MALMBORG A.C.,
MICHAËLSSON A.,
OHLIN M.,
JANSSON B.,
BORREBAECK C. A. K.
Publication year - 1992
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1992.tb02970.x
Subject(s) - chemistry , monoclonal antibody , reaction rate constant , antibody , surface plasmon resonance , biosensor , dissociation constant , kinetics , dissociation (chemistry) , dissociation rate , antigen , microbiology and biotechnology , chromatography , biochemistry , biology , immunology , materials science , receptor , physics , quantum mechanics , nanoparticle , nanotechnology
Surface plasmon resonance, i.e. detection of changes in refractive index on a surface, was used in a biosensor to evaluate the dissociation/association rate and affinity constants of human monoclonal IgG and IgM antibodies and Tab fragments. The results showed that an observed difference in affinity constants between intact and fragmented IgG anti‐tetanus antibody was related to approximately 10‐fold differences in dissociation rate constants, since the association rate constants were in the same range, i.e. 2–3×10 5 ( m ‐1 s ‐1 ). Affinity constants, as determined by conventional solid phase enzyme immunoassays, were substantially higher than the constants produced by the biosensor. Human monoclonal IgM anti‐Tnα antibodies showed, furthermore, one order of magnitude higher association rate constants, as compared with the IgG antibodies, but since the dissociation rate constants were more than ten times higher, the resulting affinity constants of the anti‐carbohydrate IgM antibodies were still somewhat lower than those of the IgG antibodies.