The adsorption of bovine serum albumin (BSA) was carried out onto polyvinyl alcohol-coated glass powder surfaces. The adsorbed amount was about four times more than that on uncoated glass. The kinetics of the adsorption process was followed colorimetrically, and kinetic parameters, such as adsorption coefficient, rate constants for adsorption and desorption, diffusion constant, and penetration rate constant, were evaluated. The effects of experimental conditions, such as pH, presence of salts, addition of aliphatic alcohols, and variation in the dielectric constant of the medium, on the amount of adsorbed BSA were investigated. The effect of temperature on adsorption was also studied, and several thermodynamic parameters, such as standard free energy change (Delta G degrees), heat of reaction (Delta H degrees), and entropy change (Delta S degrees), were evaluated.