Comparison of weak strong high-performance anion-exchange chromatography

A comparison of the chromatographic characteristics of weak anion exchangers with those of strong anion exchangers was made for a series of proteins. On both SynChropak AX300 Q300 the resolution of bovine serum albumin from its dimer was better at pH 6 than at pH 8. Conversely, catalase components separated better at pH 8 than at pH 6. A pH effect which may be due to hydrophobicity was observed for ovalbumin lactate dehydrogenase on the weak anion exchangers. A protein with a molecular weight of 140 000 shows equivalent separations on both 300-Å 1000-Å column materials, whereas smaller proteins are fractionated better on the 300-Å columns.