MULTIPLE PEAKS IN HIGH-PERFORMANCE LIQUID-CHROMATOGRAPHY OF PROTEINS - BETA-LACTOGLOBULINS ELUTED IN A HYDROPHOBIC INTERACTION CHROMATOGRAPHY SYSTEM

The chromatographic behavior of beta-lactoglobulins when eluted in hyd rophobic interaction chromatography systems is studied. By modifying s ome factors, such as pH and temperature, the relationship between shap e of the chromatographic peak and protein structure is shown. At pH 4. 5 and low temperature multiple peaks for beta-LG A and beta-LG B are o bserved and assigned to aggregates. The effects of other parameters, b esides pH and temperature, such as volume and concentration of injecte d sample, contact time between protein and stationary and/or mobile ph ases, and nature and concentration of mobile phase upon aggregation ar e studied. Comparison of the chromatographic behavior of both variants of beta-lactoglobulin is made. (C) 1997 Elsevier Science B.V.