Abstract
A kinetic equation describing two consecutive adsorption steps was derived by considering the diffusion-controlled step followed by the energy barrier-controlled step. A novel method to evaluate the interfacial pressure of protein solution on polymer membrane surface as a function of time was developed. The adsorption behavior of bovine serum albumin and bovine serum γ-globulin onto block and random polyaminoacid copolymer membrane surface was investigated by using the equation and experimental method developed. Comparison of adsorption behavior was made on block and random copolymers composed of γ-benzyl-l-glutamate and l-leucine, and partly hydrophilic polyaminoacid of different OH contents which were prepared by aminoalcoholysis of the parent block copolymer. The effective cross-sectional area A of albumin (ca. 600 A2) was about three times of γ-globulin (ca. 200 A2) for both block and random copolyaminoacids. The Fab portion of γ-globulin seemed to be oriented toward hydrophilic surface, in contrast to the orientation of Fc portion toward hydrophobic surface.
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