Miscibility gap of octyl glucoside-phosphatidylcholine micellar solutions. Partition of the nicotinic acetylcholine receptor into the surfactant-rich phase

Schürholz, Theo; Gieselmann, Anke; Neumann, Eberhard

doi:10.1016/0005-2736(89)90471-9

Cited by 16 publications

(11 citation statements)

References 26 publications

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“…This has been extensively studied for detergents of the Triton family (9). Other additives like glycerol or urea strongly affect the phase behavior of a detergent, as does the presence of lipids in mixed micelles (10) and the addition of polymers (see next section).…”

Section: Phase Diagramsmentioning

confidence: 99%

“…This can be exploited for the purification of membrane proteins, using PEG (or dextran) with -octylglucoside (-OG), -dodecyl-maltoside (17,36), or -octylthioglu-coside (-OTG) (37,38). Depending on the ratio of detergent and lipid, phase separation of -OG can occur during membrane solubilization without the addition of polymers and has been used to purify nicotinic acetylcholine receptor (10). …”

Section: Glycosidic Detergentsmentioning

confidence: 99%

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Phase Separation in the Isolation and Purification of Membrane Proteins

Arnold

Linke

2007

BioTechniques

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Phase separation is a simple, efficient, and cheap method to purify and concentrate detergent-solubilized membrane proteins. In spite of this, phase separation is not widely used or even known among membrane protein scientists, and ready-to-use protocols are available for only relatively few detergent/membrane protein combinations. Here, we summarize the physical and chemical parameters that influence the phase separation behavior of detergents commonly used for membrane protein studies. Examples for the successful purification of membrane proteins using this method with different classes of detergents are provided. As the choice of the detergent is critical in many downstream applications (e.g., membrane protein crystallization or functional assays), we discuss how new phase separation protocols can be developed for a given detergent buffer system.

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Section: Phase Diagramsmentioning

confidence: 99%

Section: Glycosidic Detergentsmentioning

confidence: 99%

Phase Separation in the Isolation and Purification of Membrane Proteins

Arnold

Linke

2007

BioTechniques

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“…11,12 However, applications to the separation and characterization for proteins has not yet appeared except for a few examples, which are described later. 77,78 3 Protein Partitioning in AMTPS of POEAE Surfactants…”

Section: •2 Amtps Of Various Surfactantsmentioning

confidence: 99%

Aqueous Micellar Two-Phase Systems for Protein Separation

1998

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The extractive technique for protein purification based on two-phase separation in aqueous micellar solutions (aqueous micellar two-phase system (AMTPS)) is reviewed. The micellar solution of a nonionic surfactant, such as polyoxyethylene alkyl ether, which is most frequently used for protein extraction, separates into two phases upon heating above its cloud point. The two phases consist of a surfactant-depleted phase (aqueous phase) and a surfactant-rich phase. Hydrophilic proteins are partitioned to the aqueous phase and hydrophobic membrane proteins are extracted into the surfactant-rich phase. Because of the methodological simplicity and rapidity, this technique has become an effective means, and thus has been widely used for the purification and characterization of proteins. In contrast to polyoxyethylene alkyl ether, micellar solutions of a zwitterionic surfactant, such as alkylammoniopropyl sulfate, separate below the critical temperature. Alkylglucosides can also separate into two phases upon adding water-soluble polymers. Recently, these twophase systems have been exploited for protein separation. Additionally, hydrophobic affinity ligands, charged polymers, and ionic surfactants have been successfully used for controlling the extractability of proteins in AMTPS.

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“…The type and concentration of the surfactant is chosen in order to optimize the enzyme yield in terms of activity or success in crystallization trials [2]. However, approaches that attempt to rationalize the relationship between enzyme/surfactant ratio and physicochemical properties of the system are scarce [3][4][5]. Nevertheless, since most of the data for membrane proteins in the literature are obtained using surfactant-solubilized samples, understanding the effects of surfactant on the structural properties of specific proteins is highly relevant for the evaluation and interpretation of experimental results.…”

Section: Introductionmentioning

confidence: 99%