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Volumn 389, Issue 2, 2009, Pages 97-101

Microcalorimetric study of the inhibition of butyrylcholinesterase by paraoxon

Author keywords

Butyrylcholine; Butyrylcholinesterase; Irreversible inhibition; Microcalorimetry; Paraoxon

Indexed keywords

ENZYMES; IMPULSE RESPONSE; KINETIC PARAMETERS; KINETIC THEORY; PHOSPHORUS COMPOUNDS; RATE CONSTANTS; SIMULATED ANNEALING; STOCHASTIC MODELS;

EID: 67349115699     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2009.03.041     Document Type: Article
Times cited : (4)

References (20)
  • 1
    • 33846784083 scopus 로고    scopus 로고
    • Calorimetry of enzyme-catalyzed reactions
    • Bianconi M.L. Calorimetry of enzyme-catalyzed reactions. Biophys. Chem. 126 (2007) 59-64
    • (2007) Biophys. Chem. , vol.126 , pp. 59-64
    • Bianconi, M.L.1
  • 2
    • 0035884687 scopus 로고    scopus 로고
    • Enzyme kinetics determined using calorimetry: a general assay for enzyme activity?
    • Todd M.J., and Gomez J. Enzyme kinetics determined using calorimetry: a general assay for enzyme activity?. Anal. Biochem. 296 (2001) 179-187
    • (2001) Anal. Biochem. , vol.296 , pp. 179-187
    • Todd, M.J.1    Gomez, J.2
  • 3
    • 32744474969 scopus 로고
    • Use of flow microcalorimetry for the determination of cholinesterase activity and its inhibition by organophosphorus pesticides
    • Konickova J., and Wadsö I. Use of flow microcalorimetry for the determination of cholinesterase activity and its inhibition by organophosphorus pesticides. Acta Chem. Scand. 25 (1971) 2360-2362
    • (1971) Acta Chem. Scand. , vol.25 , pp. 2360-2362
    • Konickova, J.1    Wadsö, I.2
  • 4
    • 15944407828 scopus 로고
    • Application of flow microcalorimetry to analytical problems: I. Determination of organophosphorus pesticides by inhibition of cholinesterase
    • Beezer A.E., and Stubbs C.D. Application of flow microcalorimetry to analytical problems: I. Determination of organophosphorus pesticides by inhibition of cholinesterase. Talanta 20 (1973) 27-31
    • (1973) Talanta , vol.20 , pp. 27-31
    • Beezer, A.E.1    Stubbs, C.D.2
  • 5
    • 33745184855 scopus 로고    scopus 로고
    • Flow microcalorimetric study of butyrylcholinesterase kinetics and inhibition
    • Debord J., Verneuil B., Bollinger J.-C., Merle L., and Dantoine T. Flow microcalorimetric study of butyrylcholinesterase kinetics and inhibition. Anal. Biochem. 354 (2006) 299-304
    • (2006) Anal. Biochem. , vol.354 , pp. 299-304
    • Debord, J.1    Verneuil, B.2    Bollinger, J.-C.3    Merle, L.4    Dantoine, T.5
  • 6
    • 37549009507 scopus 로고    scopus 로고
    • Microcalorimetric study of the inhibition of butyrylcholinesterase by carbamates
    • Debord J., Laubarie C., and Dantoine T. Microcalorimetric study of the inhibition of butyrylcholinesterase by carbamates. Anal. Biochem. 373 (2008) 247-252
    • (2008) Anal. Biochem. , vol.373 , pp. 247-252
    • Debord, J.1    Laubarie, C.2    Dantoine, T.3
  • 7
    • 15944409551 scopus 로고    scopus 로고
    • Flow microcalorimetric study of enzyme reactions: application to arylesterase from human serum
    • Debord J., Harel M., Bollinger J.-C., Verneuil B., Merle L., and Dantoine T. Flow microcalorimetric study of enzyme reactions: application to arylesterase from human serum. Thermochim. Acta 427 (2005) 85-91
    • (2005) Thermochim. Acta , vol.427 , pp. 85-91
    • Debord, J.1    Harel, M.2    Bollinger, J.-C.3    Verneuil, B.4    Merle, L.5    Dantoine, T.6
  • 9
    • 0032573399 scopus 로고    scopus 로고
    • A putative kinetic model for substrate metabolisation by Drosophila acetylcholinesterase
    • Stojan J., Marcel V., Estrada-Mondaca S., Klaebe A., Masson P., and Fournier D. A putative kinetic model for substrate metabolisation by Drosophila acetylcholinesterase. FEBS Lett. 440 (1998) 85-88
    • (1998) FEBS Lett. , vol.440 , pp. 85-88
    • Stojan, J.1    Marcel, V.2    Estrada-Mondaca, S.3    Klaebe, A.4    Masson, P.5    Fournier, D.6
  • 10
    • 0000169232 scopus 로고
    • An algorithm for least squares estimation of nonlinear parameters
    • Marquardt D.W. An algorithm for least squares estimation of nonlinear parameters. J. Soc. Industr. Appl. Math. 11 (1963) 431-441
    • (1963) J. Soc. Industr. Appl. Math. , vol.11 , pp. 431-441
    • Marquardt, D.W.1
  • 11
    • 0017347893 scopus 로고
    • Cholinesterase inhibition studies by stopped-flow instrumentation and automated data processing
    • Horton G.L., Lowe J.R., and Lieske C.N. Cholinesterase inhibition studies by stopped-flow instrumentation and automated data processing. Anal. Biochem. 78 (1977) 213-228
    • (1977) Anal. Biochem. , vol.78 , pp. 213-228
    • Horton, G.L.1    Lowe, J.R.2    Lieske, C.N.3
  • 12
    • 0015789712 scopus 로고
    • Recording spectrophotometric method for determination of dissociation and phosphorylation constants for the inhibition of acetylcholinesterase by organophosphates in the presence of substrate
    • Hart G.J., and O'Brien R.D. Recording spectrophotometric method for determination of dissociation and phosphorylation constants for the inhibition of acetylcholinesterase by organophosphates in the presence of substrate. Biochemistry 12 (1973) 2940-2945
    • (1973) Biochemistry , vol.12 , pp. 2940-2945
    • Hart, G.J.1    O'Brien, R.D.2
  • 13
    • 0020436442 scopus 로고
    • Identification of isoenzymes in cholinesterase preparations using kinetic data of organophosphate inhibition
    • Chemnitius J.M., Haselmeyer K.H., and Zech R. Identification of isoenzymes in cholinesterase preparations using kinetic data of organophosphate inhibition. Anal. Biochem. 125 (1982) 442-452
    • (1982) Anal. Biochem. , vol.125 , pp. 442-452
    • Chemnitius, J.M.1    Haselmeyer, K.H.2    Zech, R.3
  • 15
  • 16
    • 34248510057 scopus 로고    scopus 로고
    • Concentration-dependent interactions of the organophosphates chlorpyrifos oxon and methyl paraoxon with human recombinant acetylcholinesterase
    • Kaushik R., Rosenfeld C.A., and Sultatos L.G. Concentration-dependent interactions of the organophosphates chlorpyrifos oxon and methyl paraoxon with human recombinant acetylcholinesterase. Toxicol. Appl. Pharmacol. 221 (2007) 243-250
    • (2007) Toxicol. Appl. Pharmacol. , vol.221 , pp. 243-250
    • Kaushik, R.1    Rosenfeld, C.A.2    Sultatos, L.G.3
  • 17
    • 0002608889 scopus 로고    scopus 로고
    • Digital iterative deconvolution procedure (DIDP) and its smoothing properties to treat with experimental spectra
    • Efimov Y.Y. Digital iterative deconvolution procedure (DIDP) and its smoothing properties to treat with experimental spectra. Vibrat. Spectrosc. 23 (2000) 57-69
    • (2000) Vibrat. Spectrosc. , vol.23 , pp. 57-69
    • Efimov, Y.Y.1
  • 18
    • 0035980703 scopus 로고    scopus 로고
    • A simple algorithm for spectral line deconvolution
    • Petrov G.M. A simple algorithm for spectral line deconvolution. J. Quant. Spectrosc. Radiat. Transfer 72 (2002) 281-287
    • (2002) J. Quant. Spectrosc. Radiat. Transfer , vol.72 , pp. 281-287
    • Petrov, G.M.1
  • 19
    • 11244344057 scopus 로고    scopus 로고
    • On deconvolution problems: numerical aspects
    • Ramm A.G., and Smirnova A.B. On deconvolution problems: numerical aspects. J. Comput. Appl. Math. 176 (2005) 445-460
    • (2005) J. Comput. Appl. Math. , vol.176 , pp. 445-460
    • Ramm, A.G.1    Smirnova, A.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.