PROTEIN ADSORPTION ON POLY(ETHYLENE-TEREPHTHALATE) TRACK MEMBRANES MODIFIED WITH GAMMA-AMINOPROPYLTRIETHOXYSILANE

The adsorption of various proteins on PET track membranes is studied a s dependent on the structural parameters of the membranes. The membran e surface is modified with gamma-aminopropyltriethoxysilane. The high adsorption of the basic proteins lysozyme and cytochrome C, and neutra l proteins gamma-globulin and hemoglobin on the modified membranes dep ends upon the ratio between the sizes of membrane pores and protein gl obules. The adsorption of acidic proteins (bovine serum albumin, ferri tin, ovalbumin, and pepsin) is about zero. The adsorption of basic and , to a lesser degree, of neutral proteins is reduced by membrane modif ication. Acidic proteins are insignificantly adsorbed on the membranes with amino groups grafted at the surface.