Surface properties of "jellyfish" : Langmuir monolayer and Langmuir-Blodgett film studies of recombinant aequorin

In this paper, we studied the surface properties of recombinant aequorin at the air-water interface. Using the Langmuir monolayer technique, the surface properties of aequorin were studied, including the surface pressure and surface potential-area isotherms, compression-decompression cycles, and sta...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1992. - 23(2007), 14 vom: 03. Juli, Seite 7602-7
1. Verfasser: Wang, Chengshan (VerfasserIn)
Weitere Verfasser: Micic, Miodrag, Ensor, Mark, Daunert, Sylvia, Leblanc, Roger M
Format: Aufsatz
Sprache:English
Veröffentlicht: 2007
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, N.I.H., Extramural Research Support, U.S. Gov't, Non-P.H.S. Apoproteins Buffers Luminescent Agents Recombinant Proteins apoaequorin Water 059QF0KO0R mehr... Aequorin 50934-79-7 Potassium Chloride 660YQ98I10 Calcium Chloride M4I0D6VV5M
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245 1 0 |a Surface properties of "jellyfish"  |b Langmuir monolayer and Langmuir-Blodgett film studies of recombinant aequorin 
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500 |a Date Revised 21.11.2013 
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520 |a In this paper, we studied the surface properties of recombinant aequorin at the air-water interface. Using the Langmuir monolayer technique, the surface properties of aequorin were studied, including the surface pressure and surface potential-area isotherms, compression-decompression cycles, and stability on Trizma Base (Tris/HCl) buffer at pH 7.6. The results showed that aequorin formed a stable Langmuir monolayer and the surface pressure-area isotherms were dependent on both pH and ionic strength. At a pH higher or lower than 7.6, the limiting molecular area decreased. The circular dichroism (CD) spectra of aequorin in aqueous solutions explained this result: when the pH was higher than 7.6, the alpha-helix conformation changed to unordered structures, whereas at a pH lower than 7.6, the alpha-helix conformation changed to beta-sheet. The addition of calcium chloride to the Tris/HCl buffer subphase (pH 7.6) caused an increase of the limiting molecular area of the aequorin Langmuir monolayer. The fluorescence spectra of a Langmuir-Blodgett (LB) film of aequorin in the presence of calcium chloride indicated that the aequorin transformed to the apoaequorin 
650 4 |a Journal Article 
650 4 |a Research Support, N.I.H., Extramural 
650 4 |a Research Support, U.S. Gov't, Non-P.H.S. 
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650 7 |a Luminescent Agents  |2 NLM 
650 7 |a Recombinant Proteins  |2 NLM 
650 7 |a apoaequorin  |2 NLM 
650 7 |a Water  |2 NLM 
650 7 |a 059QF0KO0R  |2 NLM 
650 7 |a Aequorin  |2 NLM 
650 7 |a 50934-79-7  |2 NLM 
650 7 |a Potassium Chloride  |2 NLM 
650 7 |a 660YQ98I10  |2 NLM 
650 7 |a Calcium Chloride  |2 NLM 
650 7 |a M4I0D6VV5M  |2 NLM 
700 1 |a Micic, Miodrag  |e verfasserin  |4 aut 
700 1 |a Ensor, Mark  |e verfasserin  |4 aut 
700 1 |a Daunert, Sylvia  |e verfasserin  |4 aut 
700 1 |a Leblanc, Roger M  |e verfasserin  |4 aut 
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