Recombinant cytochrome p450 immobilization for biosensor applications
As a result of the very attractive pleiotropic properties of the heme-enzymes, three P450 cytochrome isoforms (P4501A2, P4502B4, P450SCC) have been utilized to identify a general optimal procedure to biodevice assembly for sensing a wide range of organic substances. The Langmuir-Blodgett films appea...
| Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1992. - 20(2004), 26 vom: 21. Dez., Seite 11706-12 |
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| Weitere Verfasser: | , , |
| Format: | Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2004
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| Zugriff auf das übergeordnete Werk: | Langmuir : the ACS journal of surfaces and colloids |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Enzymes, Immobilized Recombinant Proteins Cytochrome P-450 Enzyme System 9035-51-2 Cholesterol 97C5T2UQ7J Clozapine J60AR2IKIC |
| Zusammenfassung: | As a result of the very attractive pleiotropic properties of the heme-enzymes, three P450 cytochrome isoforms (P4501A2, P4502B4, P450SCC) have been utilized to identify a general optimal procedure to biodevice assembly for sensing a wide range of organic substances. The Langmuir-Blodgett films appears to yield the best stable working conditions as shown by UV-vis spectrophotometry, nanogravimetry, circular dichroism, and electrochemical characterization, to identify the ordered nanostructures of P450 cytochromes optimal for clozapine, styrene, and cholesterol sensing. Only in the presence of low purity grade protein, as in the case of P4501A2, a gel-matrix was needed to warrant the optimal clozapine sensing. By the combination of proper immobilization, transducer and nanostructured mutants of high-grade stable and selective P450-based sensors appear capable to detect the interaction with a wide range of organic substrates such as fatty acids, drugs, and toxic compounds |
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| Beschreibung: | Date Completed 03.02.2006 Date Revised 21.11.2013 published: Print Citation Status MEDLINE |
| ISSN: | 1520-5827 |