To ensure that the protein is completely dissolved and that only one protein molecule is present in each detergent micelle, excess of detergent is often employed to solubilize membrane proteins. However, it may bring trouble to protein researchers, as excess detergent may not be desired to exist in the downstream applications. On the one hand, an excess amount of detergent presents in the samples may interfere with protein activity or concentration measurement. On the other hand, excess detergent can unfortunately complicate spectra or disrupt further experimental work. In other cases, the detergent initially used for solubilization may not be appropriate for subsequent analytical procedure. Therefore, removal of excessive or unwanted detergent is an essential step in membrane protein research.
The optimal approach for removal of detergent from protein samples depends upon the type of detergent present in the sample. In other words, corresponding methods will be used to remove detergent according to different types of detergent with different properties in aqueous solution such as critical micelle concentration (CMC), charge or the aggregation number. Generally, detergents with a high (>1 mM) CMC are easily removed by methods such as dialysis or through ultrafiltration membranes. Detergents with low (<1 mM) CMC should be chromatographic methods. At present, there are several commonly used detergents removal methods, including dialysis, hydrophobic adsorption, gel chromatography, ion-exchange chromatography, and nickel columns and His tags [1].
Fig. 1. Dialysis methods for detergent removal.
Fig. 2. Hydrophobic methods for detergent removal.
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