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Adsorption of bovine albumin, gamma-globulin and fibrinogen from phosphate buffer solution (pH = 7.5) onto several polymer films was studied using the radioiodinated proteins (125I). The kinetics of desorption of the proteinated polymer films in bovine plasma was determined. Contact angle measurements on these same polymers allowed the calculation of dispersive (WA d) and polar (Ip) components of the polymer-protein solution system. Results from these measurements show that the nondispersive-dispersive force balance at the polymer-protein solution interface, expressed by the Ip/WA d ratio, is an important factor for binding of proteins on polymer surfaces. The purity of fibrinogen and the cleaning procedures for the polymer surfaces influence the absolute values of proteins adsorbed on polymer surfaces.
Baszkin et al. (1980) studied this question.