Abstract
The homogeneous exchange process whereby IgG molecules adsorbed onto latex particles are replaced by IgG molecules from the bulk solution was studied by means of 125I radiolabeling. The exchange mechanism was investigated on surfaces saturated with either labeled or unlabeled proteins in the presence of a solution of the opposite species in two sets of independent experiments. After rinsing of the surface by pure buffer followed by supplementary IgG adsorption, the exchange process followed a kinetic law of first order with respect to the IgG molecules from the bulk solution, and the apparent exchange rate constant was (2.3 +/- 0.4) x 10(-5) cm.hr-1.
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