STUDIES ON ADSORPTION-ISOTHERMS OF PROTEINS ON HYDROPHOBIC SURFACE

Adsorption isotherms of proteins on hydrophobic surface were measured by frontal chromatography. It was found the adsorption isotherms of lysozyme and bovine serum albumin to be linear and those of cytochrome-c, myoglobin, insulin, alpha-amylase, and ovalbumin to be convex. With the comparison among stoichiometric displacement model of adsorption (SDM-A), the Langmuir model, the BET equation, and the Jovanovic equation, the first one was found to fit two kinds of adsorption isotherms mentioned above well, the second one could only be used to describe the fatter well, while the last two equations could not be used to describe anyone of them well. Far ovalbumin, the linear parameters of the SDM-A and the Langmuir model were found to have certain regularity with the changes in the concentrations of ammonium sulfacte.