Ionic effects in the chromatography of proteins on columns of controlled-pore glass

Bovine serum albumin, acetylcholinesterase and two non-protein markers were chromatographed on columns of controlled-pore glasses in buffer solutions of varied ionic strengths. Adsorption of protein to the glass and ionic effects due to repulsion of the negatively-charged solutes from the glass matrix were observed. When glasses were treated with Carbowax 20M, the adsorption disappeared but ion exclusion effects persisted. The ionic behavior of Carbowax-treated glasses was similar to that observed by one of the authors when using agarose columns.