Hydrophobic interaction chromatograph

Hydrophobic interaction chromatograph (HIC), while very attractive in principle, has proved difficult to scale up for processing. A recent series of articles explores some of the unique problems associated with process-scale HIC. Load sample preparation20 must be carefully examined to prevent protein aggregate formation in the presence of the relatively high salt concentrations used in this technique. Successful scale-up also requires the setting of wide specifications to accomodate routine variations in the feed.21 The effect of the salt concentration on capacity may be somewhat more... 

The most popular hydrophobic interaction chromatographic beads (resins) are cross-linked agarose gels to which hydrophobic groups have been covalently linked. Specific examples include... 

As noted in Section VIII, preparative ion-exchange and hydrophobic interaction chromatographic procedures have come to occupy, from practical considerations, central positions in the fractionation of protein mixtures, typically enabling purification factors in the range of 10- to 100-fold.6,364,366... 

Ferreira, I.M.P.L.V.O. Mendes, E. Ferreira, M.A. HPLC/UV analysis of proteins in dairy products using a hydrophobic interaction chromatographic column. Analytical Sciences, 2001,17, 499-501. 

Despite the intrinsically nonspecific nature of ion-exchange and reversed-phase/hydrophobic interactions, it is often found that chromatographic techniques based on these interactions can exhibit remarkable resolution this is attributed to the dynamics of multisite interactions being different for proteins having differing surface distributions of hydrophobic and/or ionizable groups. 

Small peptides may be difficult to chromatograph by aqueous GFC due to complex nonsize effects such as ionic and hydrophobic interactions. Elution... 

After initial cell fermentation and product extraction from the producer cells, the crude preparation is subject to multiple chromatographic steps, including ion-exchange, hydrophobic interaction chromatography and gel-filtration chromatography. The purified product is presented in lyophilized form in vials (1 mg active/vial) and excipients include a phosphate buffer, sodium chloride and serum albumin. 

A common feature of protein retention in reversed-phase and other interactive chromatographic modes such as ion exchange and hydrophobic interaction... 

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