Hydrophobic interaction chromatography glycoproteins

Figure 6 Hydrophobic interaction chromatography of serum glycoproteins on a TSK Phenyl 5-PW column (0.75 x 7.5 cm). The proteins are eluted at a flow rate of 1.0 mL/min with a gradient of decreasing salt concentration, from 1.7 M ammonium sulfate in 0.1 M sodium phosphate buffer, pH 7.0 to 0.01 M sodium phosphate buffer, pH 7.0 during 30 min. In the case of LRG, water was used for elution of the protein after 40 min. Because of the low grade of ammonium sulfate used, the baseline decreased gradually with the decrease of the salt concentration. The ceruloplasmin peak observed at 610nm indicates that the protein can retain blue copper during the chromatography.

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