Abstract
ABSTRACT Reversible and irreversible aspects of polyclonal IgG adsorption onto glass beads were studied using 125I radiolabeled proteins for bulk concentrations as low as 4× 10−4 mg ml−1. A true thermodynamic equilibrium was reached in the low bulk concentration domain, and a saturation of 0.1μg cm−2 was noticed for concentrations ranging from 0.03 to 0.37mg ml−1. The decrease of the amount of desorbed IgG's with increasing bulk concentrations in the plateau domain taken together with the impossibility to adjust desorption kinetics using a single exponential law, allowed us to propose an adsorption mechanism in which two protein populations i.e. rapidly (state B) and slowly (state C) desorbed molecules are involved
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