VZL 2010, 79(1):9-14

Colorimetric Detectors Based on Acetylcholinesterase and Its Construction

Miroslav Pohanka ORCID...1,2, Vítězslav Vlček3, Jana Žďárová Karasová ORCID...2, Kamil Kuča ORCID...1,2, Jiří Cabal2
1 Univerzita obrany, Fakulta vojenského zdravotnictví, Centrum pokročilých studií, Hradec Králové
2 Univerzita obrany, Fakulta vojenského zdravotnictví, katedra toxikologie, Hradec Králové
3 Mendelova zemědělská a lesnická univerzita, Agronomická fakulta, Ústav agrochemie, půdoznalství, mikrobiologie a výživy rostlin, Brno

Kolorimetrické detektory založené na rekogniční schopnosti acetylcholinesterasy (AChE) jsou vhodným nástrojem pro rychlou a přitom vysoce senzitivní detekci nervově paralytických látek a některých pesticidů založené na inhibici AChE. V tomto přehledovém článku jsou nastíněny základní biochemické metody vhodné pro kolorimetrické stanovení aktivity AChE. Zároveň jsou popsány matrice vhodné pro konstrukci vlastních průkazníků a chemické i fyzikální metody vazby AChE na jejich povrch. Detehit a ChP-71 jsou uvedeny jako typické kolorimetrické detektory pro stanovení nervově paralytických látek.

Keywords: Kolorimetrie; Nervově paralytická látka; Acetylcholinesterasa; Průkazník; Detektor

Colorimetric detectors based on recognition capability of acetylcholinesterase (AChE) are a suitable tool for fast but sensitive detection of nerve agents and some pesticides based on AChE inhibition. In this review article, basic biochemical methods appropriate for colorimetric estimation of AChE enzymatic activity are presented. Moreover, the available matrices suitable for construction of dipsticks and chemical as well as physical immobilization protocols for AChE binding on matrice surface are described, too. Detehit and ChP-71 are indicated as typical colorimetric detectors for assay of nerve agents.

Keywords: Colorimetry; Nerve agents; Acetylcholinesterase; Dipstick; Detector

Received: November 5, 2009; Published: March 1, 2010  Show citation

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Pohanka, M., Vlček, V., Žďárová Karasová, J., Kuča, K., & Cabal, J. (2010). Colorimetric Detectors Based on Acetylcholinesterase and Its Construction. Vojenské Zdravotnické Listy79(1), 9-14
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References

  1. ANDREESCU, S. - BARTHELMEBS, L. - MARTY, JL. Immobilization of acetylcholinesterase on screen-printed electrodes: comparative study between three immobilization methods and applications to the detection of organophosphorus insecticides. Anal. Chim. Acta, 2002, vol. 464, no. 2, p. 171-180. Go to original source...
  2. ARDUINI, F. - RICCI, F. -TUTA, CS., et al. Detection of carbamic and organophosphorous pesticides in water samples using a cholinesterase biosensor based on Prussian Blue-modified screen-printed electrode. Anal. Chim. Acta, 2006 vol. 580, no. 2, p. 155-162. Go to original source... Go to PubMed...
  3. BOTTCHER, H. - SOLTMANN, U. - MERTIG, M., et al. Biocers: ceramics with incorporated microorganisms for biocatalytic, biosorptive and functional materials development. J. Materials Chemistry, 2004, vol. 14, no. 14, p. 2176-2188. Go to original source...
  4. CASIDA, JE. - QUISTAD, GB. Serine hydrolase targets of organophosphorus toxicants. Chem. Biol. Interact., 2005, vol. 157, no. 158, p. 277-283. Go to original source... Go to PubMed...
  5. CHO, YA. - LEE, HS. - CHA, GS., et al. Fabrication of butyrylcholinesterase sensor using polyuretane-based ion-selective membranes. Biosensors & Bioelectronics, 1999, vol. 14, p. 435-438. Go to original source... Go to PubMed...
  6. CUI, G. - KIM, SJ. - CHOI, SH., et al. A disposable amperometric sensor screen printed on a nitrocellulose strip: a glucose biosensor employing lead oxide as an interference-removing agent. Anal. Chem., 2000, vol. 72, no. 8, p. 1925-1929. Go to original source... Go to PubMed...
  7. GUERRIERI, A. - MONACI, L. - QUINTO, M., et al. A disposable amperometric biosensor for rapid screening of antichoinesterase aktivity in soil extracts. Analyst, 2002, vol. 127, no. 1, p. 5-7. Go to original source... Go to PubMed...
  8. NO, HY. - KIM, YA. - LEE, YT., et al. Cholinesterase-based dipstick assai for the detection of organophosphate and carbamate pesticides. Anal. Chim. Acta, 2007, vol. 594, no. 1, p. 37-43. Go to original source... Go to PubMed...
  9. PATOČKA, J. - KUČA, K. - JUN, D. Acetylcholinesterase and butyrylcholinesterase - important enzymes of human body. Acta Medica, 2004, vol. 47, no. 4, p. 215-228. Go to original source... Go to PubMed...
  10. POHANKA, M. - MUSILEK, K. - KUČA, K. Progres sof biosensors based on cholinesterase inhibition. Curr. Med. Chem., 2009, vol. 16, no. 14, p. 1790-1798. Go to original source... Go to PubMed...
  11. SANCHEZ, S. - PUMERA, M. - CABRUJA, E., et al. Carbon nanotube/polysulfone composite screen-printed electrochemical enzyme biosensors. Analyst, 2007, vol. 132, no. 2, p. 142-147. Go to original source... Go to PubMed...
  12. SANTHA, H. - DOBAY, R. - HARSANYI, G. Amperometric uric acid biosensors fabricated of various types of uricase enzymes. IEEE Sensors J., 2003 vol. 3, no. 3, p. 282-287. Go to original source...
  13. SOTIROPOULOU, S. - CHANIOTAKIS, NA. Lowering the detection limit of the acetylcholinesterase biosensor using a nanoporous carbon matrix. Anal. Chim. Acta, 2005, vol. 530, no. 2, p. 199-204. Go to original source...
  14. TIMUR, S. - TELEFONCU, A. Acetylcholinesterase (AChE) electrodes based on gelatin and chitosan matrices for the pesticide detection. Artif. Cell Blood Substit. Immobil. Biotechnol., 2004, vol. 32, no. 3, p. 427-442. Go to original source... Go to PubMed...
  15. WANG, S. - LI, S. - YU, Y. Immobilization of cholesterol oxidase on celulose acetate membráně for free cholesterol biosensor development. Artif. Cells Blood Substit. Immobil. Biotechnol., 2004, vol. 32, no. 3, p. 413-425. Go to original source... Go to PubMed...
  16. ZHANG, J. - LUO, A. - LIU, P., et al. Detection of organophosphorus pesticides using potentiometric enzymatic membráně biosensor based on methylcellulose immobilization. Anal. Sci., 2009, vol. 25, no. 4, p. 511-515. Go to original source... Go to PubMed...