EVALUATION OF TERPOLYMERS OF 2-HYDROXYETHYL METHACRYLATE, DODECYL METHACRYLATE AND ETHYLENE-GLYCOL DIMETHACRYLATE AS MATRICES FOR HYDROPHOBIC INTERACTION CHROMATOGRAPHY

Polymer matrices were prepared by suspension polymerization of 2-hydro xyethyl methacrylate, dodecyl methacrylate and ethylene glycol dimetha crylate. It was shown that porosity decreased with the addition of mon omers with hydrophobic side chains. Trypsin, bovine serum albumin and lipase served as standard proteins in sorbent hydrophobicity evaluatio n. Isocratic chromatography at various ionic strengths revealed differ ent elution behaviours. Some sorbents exhibited an ion-exchange mode i n the whole range of ionic strength variation. Some others showed a hy drophobic interaction character when the salt concentration exceeded a critical value. It is suggested to take this critical salt concentrat ion as a relative measure of hydrophobicity for particular protein-mat rix-salt systems. It was shown that the matrix containing 90 mu mol/g of dodecyl methacrylate was enough hydrophobic to differentiate protei ns and thus could be used effectively for hydrophobic interaction chro matography of proteins.