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Cromatography Handbook of HPLC - Rizzi A.

Rizzi A. Cromatography Handbook of HPLC - John Wiley & Sons, 2005. - 14 p.
Download (direct link): chromatographyhandbook2005.pdf
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Biopolymers
Ziad El Rassi
Oklahoma State University, Stillwater, Oklahoma
I. INTRODUCTION
Hydrophobic interaction chromatography (ͲÑ), employing weakly hydrophobic sorbents and descending salt gradients, is exclusively used in the separation of large biomacromolecules and, in particular, proteins. Solute retention is based on the noncovalent association between the nonpolar moieties of the biopolymer solute and the weakly hydrophobic ligand of the stationary phase. This association is driven by the use of aqueous mobile phases of high-ionic strengths. Usually, the stationary phase consists of a highly hydrophobic organic layer to which widely spaced, short alkyl or small aryl functions are attached. This rather “friendly environment” induces little or no irreversible protein unfolding, thereby making Í²Ñ a nondenaturing chromatographic method highly suited for the purification of bioactive proteins. In other words, the energetically “soft” stationary phases usually do not undergo strong interactions with internal hydrophobic residues in the protein molecule.
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