Size exclusion detergent

Aqueous-detergent solutions of appropriate concentration and temperature can phase separate to form two phases, one rich in detergents, possibly in the form of micelles, and the other depleted of the detergent (Piyde and Phillips, op. cit.). Proteins distribute between the two phases, hydrophobic (e.g., membrane) proteins reporting to the detergent-rich phase and hydrophilic proteins to the detergent-free phase. Indications are that the size-exclusion properties of these systems can also be exploited for viral separations. These systems would be handled in the same way as the aqueous two-phase systems. 

Figure 3. Size exclusion chromatography analysis of AP-trapped vs. detergent-solubilized FS2 core complexes.

A detergent may be added to aqueous systems to prevent tailing and sometimes size-exclusion chromatography may require a fungicide to prevent fungal growth. Gases and suspended matter can render a gel column completely useless. 

Ion-retardation resins, which consist of acrylic acid polymerized inside a strong anion-exchange resin on a polystyrene divinylbenzene matrix [30], are also effective for removal of SDS from proteins. Passage of a protein-SDS complex through the resin results in complete retention of SDS and elution of protein with 80-90% recovery [31]. The capacity of the resin for SDS is more than 2.2mg/g, which effectively reduces the SDS level to less than one molecule of SDS per protein molecule. Because SDS binds tenaciously to the resin, it cannot be removed and the resin must be discarded after use. In the presence of buffers, adsorption of SDS by an ion-retardation column is reduced, resulting in incomplete removal of detergent from the protein. This can be circumvented by prior removal of buffer by SEC or, more conveniently, by the addition of a few grams of size exclusion gel to the head of the ion-retardation resin bed to retard the buffer [4]. 

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