Total internal reflection fluorescence (TIRF) and ellipsometry have been used to study competitive protein adsorption to a hydrophobic model surface prepared by radio frequency plasma deposition of hexamethyl disiloxane on silicon. Single, binary, and ternary protein solutions of human serum albumin (HSA), IgG, and fibrogen (Fgn) at concentrations corresponding to 1/100 of those in blood plasma were investigated. It is shown that by employing the combination of ellipsometry and TIRF, information on both the total adsorbed amount and the composition of the adsorbed protein layer can be obtained. It was found that adsorbed HSA is not displaced by IgG and/or Fgn to any large extent. IgG and HSA dominate the adsorption from the ternary protein mixture, although fibrinogen is also present in the adsorbed layer to a smaller extent.