Application of a biosensor for super-sensitive detector of clenbuterol
We explored the potential of the motor protein F 0 F 1 -ATPase as biosensors of harmful residues in food. A fluorescence probe F1300 labelled in inner chromatophores was used as a pH indicator for detecting proton flux driven by ATP synthesis in F 0 F 1 -ATPase. Furthermore, the F 1 β subunit of F 0...
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Published in | New Zealand journal of agricultural research Vol. 50; no. 5; pp. 689 - 695 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
Taylor & Francis Group
01.12.2007
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Subjects | |
Online Access | Get full text |
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Summary: | We explored the potential of the motor protein F
0
F
1
-ATPase as biosensors of harmful residues in food. A fluorescence probe F1300 labelled in inner chromatophores was used as a pH indicator for detecting proton flux driven by ATP synthesis in F
0
F
1
-ATPase. Furthermore, the F
1
β subunit of F
0
F
1
ATPase was attached by a system of anti-β antibody-biotin-avidin-biotin-second antibody (specific for clenbuterol) as a biosensor to detect clenbuterol residues. The capturing mechanism was based on the antibody-antigen reaction, while the detecting mechanism depended on a fluorescence change responding to ph changes during the rotary catalytic ATP synthesis process. The results showed that the activity of F
0
F
1
-ATPase was affected with different loads and the new biosensor may prove to be a useful nano-device for super-sensitive (10
-12
g/litre clenbuterol) detection. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Conference-1 ObjectType-Feature-3 content type line 23 SourceType-Conference Papers & Proceedings-2 |
ISSN: | 0028-8233 1175-8775 |
DOI: | 10.1080/00288230709510339 |