Abstract
The kinetics of antibody-binding to surface-immobilized antigen was studied by ellipsometry, using bovine serum albumin as antigen. The results show that the initial binding of antibody was linear to the square root of time rather than time, indicating an initial diffusion-rate limitation of the reaction. The antibody-binding rate was retarded at a surface concentration of 0.2 μg/cm 2 and became reaction-rate limited above this surface concentration. The reverse reaction was shown to be too slow to be measured after 43 h dissociation. A Scatchard plot of the data showed time dependence which gave a further indication that the antibody-binding was not an equilibrium reaction. The results obtained from ellipsometry experiments were applied to experiments with the enzyme linked immunosorbent assay (ELISA) which by the sensitive detection system measures the initial antibody-binding to immobilized antigen. It was shown that the dose-response curve of the ELISA could be explained assuming a diffusion-rate limited, irreversible antibody-binding to the immobilized antigen.
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