Electrochemical extraction of proteins by reverse micelle formation

The transfer of proteins by the anionic surfactant bis(2-ethylhexyl) sulfosuccinate (AOT) at a polarized 1,2-dichloroethane/water (DCE/W) interface was investigated by means of ion-transfer voltammetry. When the tetrapentylammonium salt of AOT was added to the DCE phase, the facilitated transfer of...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1992. - 22(2006), 13 vom: 20. Juni, Seite 5937-44
1. Verfasser: Shinshi, Mariko (VerfasserIn)
Weitere Verfasser: Sugihara, Takayasu, Osakai, Toshiyuki, Goto, Masahiro
Format: Aufsatz
Sprache:English
Veröffentlicht: 2006
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, Non-U.S. Gov't 1,4-bis(2-ethylhexyl) sodium sulfosuccinate Ethylene Dichlorides Micelles Protamines Proteins Succinates Surface-Active Agents Water mehr... 059QF0KO0R ethylene dichloride 55163IJI47 Cytochromes c 9007-43-6 Ribonuclease, Pancreatic EC 3.1.27.5
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100 1 |a Shinshi, Mariko  |e verfasserin  |4 aut 
245 1 0 |a Electrochemical extraction of proteins by reverse micelle formation 
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500 |a Date Completed 20.07.2007 
500 |a Date Revised 21.11.2013 
500 |a published: Print 
500 |a ErratumIn: Langmuir. 2006 Sep 26;22(20):8614 
500 |a Citation Status MEDLINE 
520 |a The transfer of proteins by the anionic surfactant bis(2-ethylhexyl) sulfosuccinate (AOT) at a polarized 1,2-dichloroethane/water (DCE/W) interface was investigated by means of ion-transfer voltammetry. When the tetrapentylammonium salt of AOT was added to the DCE phase, the facilitated transfer of certain proteins, including cytochrome c (Cyt c), ribonuclease A, and protamine, could be controlled electrochemically, and a well-defined anodic wave for the transfer was obtained. At low pH values (e.g., pH 3.4), the anodic wave was usually well-separated from the wave for the formation of protein-free (i.e., unfilled) reverse micelles. The anodic wave for the protein transfer was analyzed by applying the theory for facilitated transfer of ions by charged ligands and then supplying information regarding the number of AOT anions reacting with one protein molecule and the total charge carried by the protein transfer. However, controlled-potential electrolyses performed for the transfer of Cyt c, which is red, revealed that the protein-AOT complexes were unstable in DCE and liable to aggregate at the interface when the pH of the W phase was 3.4. At pH 7.0, when formation of unfilled reverse micelles occurred simultaneously, the protein-AOT complexes appeared to be stabilized, probably via fusion with unfilled reverse micelles 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
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650 7 |a Ethylene Dichlorides  |2 NLM 
650 7 |a Micelles  |2 NLM 
650 7 |a Protamines  |2 NLM 
650 7 |a Proteins  |2 NLM 
650 7 |a Succinates  |2 NLM 
650 7 |a Surface-Active Agents  |2 NLM 
650 7 |a Water  |2 NLM 
650 7 |a 059QF0KO0R  |2 NLM 
650 7 |a ethylene dichloride  |2 NLM 
650 7 |a 55163IJI47  |2 NLM 
650 7 |a Cytochromes c  |2 NLM 
650 7 |a 9007-43-6  |2 NLM 
650 7 |a Ribonuclease, Pancreatic  |2 NLM 
650 7 |a EC 3.1.27.5  |2 NLM 
700 1 |a Sugihara, Takayasu  |e verfasserin  |4 aut 
700 1 |a Osakai, Toshiyuki  |e verfasserin  |4 aut 
700 1 |a Goto, Masahiro  |e verfasserin  |4 aut 
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