Abstract
Rates of desorption of proteins were measured by the decrease in area at a reference surface pressure of 5 mN m −1 after maintaining monolayers at higher constant pressures for given times. Kinetics followed a t 1 2 relation, consistent with a diffusion-controlled process from a subsurface layer of constant concentration. For two proteins studied, β-lactoglobulin and insulin, initial rates of desorption from mixed monolayers with nondesorbable components were the same as for the pure monolayers. Rates deviated from those of the pure monolayers only when the areas occupied by the desorbing proteins reached values near 30% of the total area. A comparison of five proteins spanning a large range of molecular weights (insulin, β-lactoglobulin, myoglobin, bovine γ-globulin, and catalase) showed that rates of desorption decreased markedly with increasing molecular weight at a given surface pressure. These results should assist in understanding transport processes across interfaces and membranes and competitive adsorption from protein mixtures in processes such as blood clotting.
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