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The combination of gradient ion exchange in the first and hydrophobic interaction chromatography in the second dimension yielded a theoretical peak capacity of 152 which is comparable to other two-dimensional chromatographic systems. Using matrices with higher efficiencies peak capacities of up to 700 are realistic. The automated protocol in its current form is able to distribute the proteins.

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Hydrophobic interaction chromatography (HIC) separates molecules based on their hydrophobicity. HIC is a useful separation technique for purifying proteins while maintaining biological activity due to the use of conditions and matrices that operate under less denaturing conditions. This section provides an overview of hydrophobic interaction chromatography with general considerations about.

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The retention of intact proteins under gradient elution in hydrophobic interaction chromatography (HIC) was found to be governed by two variables, the steady region (SR) and the migration region (MR). In the SR, the proteins are immobilized by the strong interactions with the stationary phase such that the retention time is independent of the column length. In the MR, the proteins also.

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