Abstract
l-Phenylalanine was immobilized on nylon membranes with two pore diameters (0.45 μm and 1 μm), by activation with 1,4-butanediol diglycidyl ether, and the effect of pore size on the affinity adsorption of γ-globulin studied by batch and kinetic methods. Experiment shows that adsorption on both affinity membranes obeys the Freundlich model. The accessible pore volume for adsorption of proteins on the membrane with 0.45 μm diameter pores is less than for that with 1 μm diameter pores. The adsorption capacity of affinity membranes with 1 μm diameter pores is 2.5-fold that of membranes with 0.45 μm diameter pores. Feed-rate has a larger effect on affinity adsorption on the membrane with 0.45 μm diameter pores than on that with 1 μm diameter pores. Small pores on the affinity membrane do not cause broadening of the elution peak. It is concluded that affinity interaction and separation occur mainly in the large pores, and small pore size does not favor improvement of adsorption capacity. γ-Globulin 85.1% pure can be obtained in one step from human plasma by use of the affinity membrane with 0.45 μm diameter pores.
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