Effects of ammonium sulfate and sodium chloride concentration on PEG/protein liquid-liquid phase separation

When added to protein solutions, poly(ethylene glycol) (PEG) creates an effective attraction between protein molecules due to depletion forces. This effect has been widely used to crystallize proteins, and PEG is among the most successful crystallization agents in current use. However, PEG is almost...

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Détails bibliographiques
Publié dans:Langmuir : the ACS journal of surfaces and colloids. - 1985. - 24(2008), 18 vom: 16. Sept., Seite 10345-51
Auteur principal: Dumetz, André C (Auteur)
Autres auteurs: Lewus, Rachael A, Lenhoff, Abraham M, Kaler, Eric W
Format: Article en ligne
Langue:English
Publié: 2008
Accès à la collection:Langmuir : the ACS journal of surfaces and colloids
Sujets:Journal Article Research Support, U.S. Gov't, Non-P.H.S. Salts Polyethylene Glycols 3WJQ0SDW1A Sodium Chloride 451W47IQ8X Ovalbumin 9006-59-1 Ammonium Sulfate SU46BAM238
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520 |a When added to protein solutions, poly(ethylene glycol) (PEG) creates an effective attraction between protein molecules due to depletion forces. This effect has been widely used to crystallize proteins, and PEG is among the most successful crystallization agents in current use. However, PEG is almost always used in combination with a salt at either low or relatively high concentrations. Here the effects of sodium chloride and ammonium sulfate concentration on PEG 8000/ovalbumin liquid-liquid (L-L) phase separation are investigated. At low salt the L-L phase separation occurs at decreasing protein concentration with increasing salt concentration, presumably due to repulsive electrostatic interactions between proteins. At high salt concentration, the behavior depends on the nature of the salt. Sodium chloride has little effect on the L-L phase separation, but ammonium sulfate decreases the protein concentration at which the L-L phase separation occurs. This trend is attributed to the effects of critical fluctuations on depletion forces. The implications of these results for designing solution conditions optimal for protein crystallization are discussed 
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650 4 |a Research Support, U.S. Gov't, Non-P.H.S. 
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700 1 |a Lewus, Rachael A  |e verfasserin  |4 aut 
700 1 |a Lenhoff, Abraham M  |e verfasserin  |4 aut 
700 1 |a Kaler, Eric W  |e verfasserin  |4 aut 
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