Abstract
The adsorption of a water-soluble dextran onto three particulate solids at three temperatures is described. All experiments were carried out at the physiological pH 7 using 0.1 M phosphate buffer. The type of isotherm obtained was dependent on the type of solid. A polar silica exhibited a low affinity for the polymer, whereas hydrophobic silver iodide particles exhibited a high affinity for the polymer and a polystyrene latex appeared to adsorb very little or no dextran. The adsorption of the dextran to silver iodide was shown to be reversible to dilution. It is suggested that entropy changes arising from changes in conformation of the polymer and the association of water molecules with the polymer and the surface of the particles control the adsorption of the dextran. The adsorption of a globular protein (bovine serum albumin) and the subsequent adsorption of the dextran to particles pretreated with a layer of this protein are also described. The pretreated particles exhibited a similar behavior towards dextran adsorption and indicated a weak affinity of the dextran for the surface. The similarity of the behavior of the pretreated particles towards dextran adsorption suggests that the adsorption was mainly influenced by the hydrated protein laver.
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