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...
| Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1992. - 23(2007), 14 vom: 03. Juli, Seite 7602-7 |
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| 1. Verfasser: | |
| Weitere Verfasser: | , , , |
| Format: | Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2007
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| 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... |
| Zusammenfassung: | 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 |
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| Beschreibung: | Date Completed 14.09.2007 Date Revised 21.11.2013 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1520-5827 |