Optimization of Quartz Crystal Microbalance-Precipitation Sensor Measuring Acetylcholinesterase Activity
2006
Kim, N.S. (Korea Food Research Institute, Songnam, Republic of Korea), E-mail: [email protected] | Park, I.S. (Korea Food Research Institute, Songnam, Republic of Korea) | Kim, D.K. (Korea Food Research Institute, Songnam, Republic of Korea)
The optimization of a batch-type quartz crystal microbalance (QCM)-precipitation sensor measuring acetylcholinesterase (AChE) activity was conducted. To covalently bind AChE onto the gold electrode of a QCM surface, glutaraldehyde cross-linking to a cystamine self-assembled monolayer was tried at different cystamine concentrations. At the optimum conditions of the QCM-precipitation sensor, 0.1 M potassium phosphate buffer (pH 8.0), containing 0.01% Tween 80, was used as the reaction buffer, with the enzyme amount of 5 units for immobilization and the substrate concentration of 50 mg/ml.
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