Terstappen G C, Ramelmeier R A, Kula M R
Institut für Enzymtechnologie, Heinrich-Heine-Universität Düsseldorf, Forschungszentrum Jülich, Germany.
J Biotechnol. 1993 Apr;28(2-3):263-75. doi: 10.1016/0168-1656(93)90175-m.
Aqueous solutions of nonionic polyoxyethylene detergents form two liquid phases upon temperature increase above the cloud point. One of these phases is detergent-enriched and called the coacervate phase, whereas the other is detergent-depleted. Protein partitioning in such detergent-based aqueous two-phase systems was studied systematically and quantitatively, employing a series of similar polyoxyethylene detergents and proteins of varying hydrophobicity. Increasing the detergent alkyl chain length, temperature or salt concentration leads to an increase of detergent separating into the coacervate phase and a concomitant increase of protein. The positive correlation between protein hydrophobicity and partitioning into the coacervate phase confirms that protein-detergent interactions in such systems are primarily hydrophobic. These detergent-based systems can be applied to membrane proteins as well as water-soluble proteins which possess hydrophobic domains.
