The special features of protein adsorption isotherms on silica adsorbents

The adsorption isotherms of hemoglobin, peroxidase, and beta-galactosidase on silochrome and mesoporous and biporous silicas were comparatively studied. Adsorption developed in two stages, including fast reversible protein adsorption (equilibrium was reached in t a parts per thousand currency sign 1-2 h) and a slow stage of irreversible binding in t a parts per thousand << 24 h (multipoint adsorption). The corresponding equilibrium constants were determined. The mechanism of unlimited linear association of peroxidase in the adsorption layer on the surface of silochrome was established.