Abstract
The effect of operational variables on retention, recovery and resolution was investigated in hydrophobic interaction chromatography of proteins on TSkgel Phenyl-5PW with a linear gradient comprising a decreasing salt concentration. Sodium sulphate was more effective in retaining proteins than ammonium sulphate or potassium phosphate. The effect of the eluent pH on retention was not as great as reported on other supports. The addition of an organic solvent or chaotropic agent promoted the desorption of proteins. High recovery was observed in most separations where the flow-rate, gradient time, initial ammonium sulphate concentration, isopropanol concentration in the final buffer and eluent pH were varied. The resolution was affected to different extents by the column length, flow-rate, gradient time and addition of organic solvent or chaotropic agent in the final buffer.
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