Aptamer with small molecular weight, simple structure, and easy synthesis, which can be used repeatedly and preserved for long time, has important applications in biosensor field. This article describes several commonly used methods for fixing aptamer onto the sensor surfaces, including the gold-sul
Comparison of immobilization methods for the development of an acetylcholinesterase biosensor
β Scribed by Kathrin Stein; Georg Schwedt
- Publisher
- Elsevier Science
- Year
- 1993
- Tongue
- English
- Weight
- 773 KB
- Volume
- 272
- Category
- Article
- ISSN
- 0003-2670
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β¦ Synopsis
Different methods for the immobilization of acetylcholinesterase (AChE), viz, co-cross-linking at the surface of a pH electrode, co-cross-linking in a membrane and trapping in a polyacrylamide membrane, are described The immobilization products are compared with respect to the response times, the reproducibility of the preparation and the applicability in a biosensor For detecting AChE inhibitors the suitability of the immobilization products in combination with a pH electrode was tested with the organophosphorus pesticide dichlorvos Keywords Biosensors, Enzymatic methods, Acetylcholmesterase, Dichlorvos, Immobilization methods, Pesticides So far biosensors have been mainh developed for the measurement of concentrations of biological compounds in medical analysis, e g, monitoring of blood sugar levels [1,2] Biosensors are made of a biochemical or biological component (receptor component), e g, an enzyme, antibody, cell or microorganism, and a transducer The transducer sends the signal formed by the receptor component to the transducing system For biosensor electrodes, field-effect transistors, fibre-optic devices, thermistors or piezoelectric crystals can be used as transducers [1][2][3][4] Normally the receptor component is directly coupled to the transducer [2] If acetylcholmesterase (AChE) is used as the biochemical component, the enzymatic hydrolysis of acetylcholine (ACh) produces acetic acid and choline The activity of the enzyme can be meas-Correspondence to
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