Abstract
In this article I have reviewed (blood) proteins adsorption onto synthetic polymer surfaces, i. e., onto polymeric microspheres. First, the surface characteristics of polymeric microspheres (polymer latices) were examined. As a result, hydrogel polymer layers, e. g., poly (acrylamide) (poly-AAm) and poly (2-hydroxyethyl methacrylate) (poly-HEMA) layers were found to exist on the microsphere surfaces of styrene (St) /AAm and St/HEMA copolymers (P (St/AAm) and P (St/HEMA)), respectively. Subsequently, singular and competitive protein adsorption onto polymeric microspheres was investigated as a function of pH and ionic strength, surface characteristics of microspheres, coexistent electrolyte ions. Each protein showed the maximum adsorption near its isoelectric point. The amounts adsorbed onto hydrophilic P (St/AAm) and P (St/HEMA) microspheres were much smaller than that onto hydrophobic polystyrene (PS) microsphere, particularly in the neutral and alkaline pH regions. Fibrinogen adsorbed preferentially from the protein mixture of albumin, γ-globulin, and fibrinogen. Further, the adsorbability of heat-denatured albumin was studied. Compared with the native component of the protein, the denatured components adsorbed preferentially onto microspheres.
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