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Date: 18-4-2016
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Hydrophobic interaction (HI) chromatography
HI-chromatography was discovered serendipitously when, in control experiments, ligands were omitted from the matrix/spacer arm combination. It was found that the resulting resins were nevertheless effective at separating proteins, due to hydrophobic interactions between the sample proteins and the aliphatic spacer arms. Following this discovery, HI-resins were purposefully designed to optimize the hydrophobic interaction.
Hydrophobic “bonds” are increased in strength by an increase in buffer ionic strength. HI-chromatography therefore conveniently fits into an isolation scheme, immediately after a salting out step, as the high salt levels will promote binding to the HI-resin. Proteins can subsequently be eluted by decreasing the buffer ionic strength, either in a stepwise manner or in a gradient.
References
-Dennison, C. (2002). A guide to protein isolation . School of Molecular mid Cellular Biosciences, University of Natal . Kluwer Academic Publishers new york, Boston, Dordrecht, London, Moscow .
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