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Detection of clenbuterol hydrochloride residuals in pork liver using a customized surface plasmon resonance bioanalyzer

Hu, J. (författare)
Department of Electrical Engineering, Henan Agricultural University, Zhengzhou, China; State Key Laboratory of Wheat and Maize Crop Science, Zhengzhou, China
Chen, R. (författare)
Department of Electrical Engineering, Henan Agricultural University, Zhengzhou, China
Wang, S. (författare)
Department of Electrical Engineering, Henan Agricultural University, Zhengzhou, China
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Wang, T. (författare)
Department of Electrical Engineering, Henan Agricultural University, Zhengzhou, China
Zhao, Y. (författare)
Hanan Mechancial and Electrical Vocational College, Zhengzhou, China
Li, J. (författare)
Department of Electrical Engineering, Henan Agricultural University, Zhengzhou, China
Hu, X. (författare)
School of Human Nutrition and Dietetics, McGill University, Ste-Anne-de-Bellevue, QC, Canada
Liang, Hao (författare)
Högskolan i Gävle,Avdelningen för elektronik, matematik och naturvetenskap
Zhu, J. (författare)
Department of Electrical Engineering, Henan Agricultural University, Zhengzhou, China
Sun, X. (författare)
Department of Electrical Engineering, Henan Agricultural University, Zhengzhou, China
Ma, L. (författare)
Department of Electrical Engineering, Henan Agricultural University, Zhengzhou, China
Jiang, M. (författare)
College of Life Sciences, Henan Agricultural University, Zhengzhou, China
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 (creator_code:org_t)
2015-03-23
2015
Engelska.
Ingår i: PLOS ONE. - : Public Library of Science (PLoS). - 1932-6203. ; 10:3
  • Tidskriftsartikel (refereegranskat)
Abstract Ämnesord
Stäng  
  • A surface plasmon resonance (SPR) immunoassay with an immobilization of self-assembled molecular identification membrane for the detection of residual Clenbuterol Hydrochloride (CLB) in pork liver was systematically investigated and experimentally validated for its high performance. SPR immunoassay with a regular competitive inhibition assay cannot be directly verified to detect CLB residuals. In this study, the binding of Au film with mercaptopropionic acid was investigated using the known form of the strong S-Au covalent bonds formed by the chemical radical of the mercaptopropionic acid and the Au film. After that, the immunoglobulin IgG of swine (SwIgG-CLB) was bonded with the mercaptopropionic acid by covalent -CO-NH- amide bonding. The modified comprehensive analysis of how the membrane structure works was introduced together with the customized SPR bioanalyzer. In order to evaluate the performance of this biomembrane structure, the concentrations of CLBcontained solutions of 0 ng•mL-1, 10 ng•mL-1, 20 ng•mL-1, 33.3 ng•mL-1, and 40 ng•mL-1 were prepared by adding CLB reagents into the solutions of CLB antibody (Clenbuterol Hydrochloride Antibody, CLB-Ab), successively and then the response unit (RU) was measured individually. Using the data collected from the linear CCD array, the fitting curve was established with the R-Square value of 0.9929. Correspondingly, the recovery rate ranged from 88.48% to 103.21% was experimented and the limit of detection of CLB in 1.26 ng•mL-1 was obtained efficiently. It was concluded that the detection method associated with biomembrane properties is expected to contribute much to the determination of residual CLB in pork liver quantitatively by using the customized SPR bioanalyzer. © 2015 Hu et al.

Ämnesord

TEKNIK OCH TEKNOLOGIER  -- Annan teknik (hsv//swe)
ENGINEERING AND TECHNOLOGY  -- Other Engineering and Technologies (hsv//eng)

Nyckelord

3 mercaptopropionic acid
clenbuterol
drug residue
gold
immunoglobulin G
Article
biosensor
covalent bond
food analysis
immunoassay
limit of detection
liver
membrane structure
molecular recognition
pork
quantitative analysis
reproducibility
surface plasmon resonance
Suidae

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