Enzyme-catalyzed reaction of voltammetric enzyme-linked immunoassay system based on OAP as substrate |
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Authors: | Shusheng Zhang Hongyuan Chen Kui Jiao |
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Institution: | (1) Department of Chemistry, Nanjing University, 210093 Nanjing, China;(2) Department of Applied Chemistry, Qingdao Institute of Chemical Technology, 266042 Qingdao, China |
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Abstract: | Theo-aminophenol (OAP)-H2O2-horseradish peroxidase (HRP) voltammetric enzyme-linked immunoassay new system has extremely high sensitivity. HRP can be
measured with a detection limit of 6.0×1010 g/L and a linear range of 1.0×10-9-4.0×10-6 g/L. The pure product of H2O2 oxidizing OAP catalyzed by HRP was prepared with chemical method. The enzyme-catalyzed reaction has been investigated with
electroanalytical chemistry, UV/Vis spectrum, IR spectrum,13C NMR,1H NMR, mass spectrum, elemental analysis, etc. Under the selected enzyme-catalyzed reaction conditions, the oxidation product
of OAP with H2O2 catalyzed by HRP is 2-aminophenoxazine-3-one. The processes of the enzyme-catalyzed reaction and the electroreduction of
the product of the enzymecatalyzed reaction have been described.
Project supported by the National Natural Science Foundation of China (Grant No. 29775012). |
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Keywords: | o-aminophenol horseradish peroxidase voltammetry enzyme-catalysis electrochemical immunoassay |
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