The kinetics of competitive adsorption of proteins onto hexadecyltrichlorosilane coated glass (HTS-glass) from model solutions containing fluorescein isothiocyanate (FITC)-labeled human serum albumin (HSA-FITC) and gamma-globulin (HGG-FITC) were studied by total internal reflection fluorescence (TIRF) spectroscopy. The processes of displacement of HSA-FITC by HGG are independent of the conformational state of HSA adsorbed onto glass. On HTS-glass, displacement of protein is hindered by the presence of large numbers of CH3-terminated alkyl tails which induce conformational (reorientational) changes in HSA-FITC and HGG-FITC adsorbed from simple solutions. In contrast to HSA, adsorption of HGG onto HTS-glass from a simple solution is characterized by the absence of irreversible adsorption in the initial portion of the kinetic curve. Competition between HSA and HGG-FITC induces replacement of end-on adsorbed HGG-FITC on HTS-glass surface with subsequent desorption of the HGG-FITC into solution. Upon further increase in the HSA concentration in solution the competition of HSA for adsorption sites prevails, which leads to a decrease in the amount of adsorbed HGG-FITC and, consequently, to a decrease in the rate of its displacement.