Abstract
The separation by hydrophobic interaction chromatography (HIC) firstly described by Hjert6n (Hjerten 1973), is based on the differential hydrophobic surface interaction. In comparison with reversed phase chromatography (RG), a weak hydrophobic group is coupled onto the chromatographic support as stationary phase and a descending salt gradient is used as mobile phase in HIC. During the separation process by HIC the bioactive protein molecules are in an aqueous salt environment and a fractionation route is applied to isolate the bioactive protein which is similar to salting out procedures used since long for protein purification. As a result, HIC might overcome the major limitations of reversed phase chromatography, which usually induces losses of the bioactivity of the sample molecule, and keeps the separating ability depending on the hydrophobicity.
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