Journal
TALANTA
Volume 88, Issue -, Pages 711-716Publisher
ELSEVIER
DOI: 10.1016/j.talanta.2011.11.072
Keywords
PON; Arylesterase; Acridinium ester; Substrate; Chemiluminescence
Categories
Funding
- National Natural Science Foundation of China [20805060]
- Fundamental Research Funds for the Central Universities [CDJZR10220004]
- Natural Science Foundation of Chongqing China [CSTC2009BB4197]
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It was found that the hydrolysis of 9-(4-chlorophenyloxycarbonyl)-10-methylacridinium triflate (CPOCMA) could be catalyzed by recombinant human PON1. Based on this property, the CPOCMA was evaluated as a substrate for serum PUN activity assay. The apparent K-m value of a serum sample for the substrate was determined as 85 nmol/L, close to the K-m value (83 nmol/L) of rHuPON1. The interferences by other esterase such as acetylcholinerase and lipases were investigated. The NaCl and CaCl2 as PON activity enhancers were able to improve the specific signal, respectively. The rHuPON1 in presence of CaCl2 showed at least 7.8 times selectivity over acetylcholinerase and lipases. By comparing with the UV methods based on phenyl acetate and diazinon, respectively, the proposed chemiluminescent method was validated with 30 serum samples. The method based on CPOCMA allows reliable, cost-saving, and specific determination in a buffer of physiological pH. (C) 2011 Elsevier B.V. All rights reserved.
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