메뉴 건너뛰기




Volumn 406, Issue 1, 2010, Pages 94-96

Explicit reformulations of time-dependent solution for a Michaelis-Menten enzyme reaction model

Author keywords

[No Author keywords available]

Indexed keywords

CURVE FITTING;

EID: 77955843887     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2010.06.041     Document Type: Article
Times cited : (40)

References (20)
  • 3
    • 0035987898 scopus 로고    scopus 로고
    • Measurement of Michaelis constants for cytochrome P450-mediated biotransformation reactions using a substrate depletion approach
    • Obach R.S., Reed-Hagen A.E. Measurement of Michaelis constants for cytochrome P450-mediated biotransformation reactions using a substrate depletion approach. Drug Metab. Dispos. 2002, 30:831-837.
    • (2002) Drug Metab. Dispos. , vol.30 , pp. 831-837
    • Obach, R.S.1    Reed-Hagen, A.E.2
  • 4
    • 0037402223 scopus 로고    scopus 로고
    • A logarithmic approximation to initial rates of enzyme reactions
    • Lu W.P., Fei L. A logarithmic approximation to initial rates of enzyme reactions. Anal. Biochem. 2003, 316:58-65.
    • (2003) Anal. Biochem. , vol.316 , pp. 58-65
    • Lu, W.P.1    Fei, L.2
  • 5
    • 71749110914 scopus 로고    scopus 로고
    • A method to describe enzyme-catalyzed reactions by combining steady-state and time-course enzyme kinetic parameters
    • Walsh R., Martin E., Darvesh S. A method to describe enzyme-catalyzed reactions by combining steady-state and time-course enzyme kinetic parameters. Biochim. Biophys. Acta 2010, 1800:1-5.
    • (2010) Biochim. Biophys. Acta , vol.1800 , pp. 1-5
    • Walsh, R.1    Martin, E.2    Darvesh, S.3
  • 7
    • 0034841038 scopus 로고    scopus 로고
    • Quantitative analysis of the time-courses of enzyme-catalyzed reactions
    • Duggleby R.G. Quantitative analysis of the time-courses of enzyme-catalyzed reactions. Methods 2001, 24:168-174.
    • (2001) Methods , vol.24 , pp. 168-174
    • Duggleby, R.G.1
  • 8
    • 0031582628 scopus 로고    scopus 로고
    • Closed form solution for time-dependent enzyme kinetics
    • Schnell S., Mendoza C. Closed form solution for time-dependent enzyme kinetics. J. Theor. Biol. 1997, 187:207-212.
    • (1997) J. Theor. Biol. , vol.187 , pp. 207-212
    • Schnell, S.1    Mendoza, C.2
  • 9
    • 0032899689 scopus 로고    scopus 로고
    • Parameter estimation using a direct solution of the integrated Michaelis-Menten equation
    • Goudar C.T., Sonnad J.R., Duggleby R.G. Parameter estimation using a direct solution of the integrated Michaelis-Menten equation. Biochim. Biophys. Acta 1999, 1429:377-383.
    • (1999) Biochim. Biophys. Acta , vol.1429 , pp. 377-383
    • Goudar, C.T.1    Sonnad, J.R.2    Duggleby, R.G.3
  • 10
    • 5644245248 scopus 로고    scopus 로고
    • Progress curve analysis for enzyme and microbial kinetic reactions using explicit solutions based on the Lambert W function
    • Goudar C.T., Harris S.K., McInerney M.J., Suflita J.M. Progress curve analysis for enzyme and microbial kinetic reactions using explicit solutions based on the Lambert W function. J. Microbiol. Methods 2004, 59:317-326.
    • (2004) J. Microbiol. Methods , vol.59 , pp. 317-326
    • Goudar, C.T.1    Harris, S.K.2    McInerney, M.J.3    Suflita, J.M.4
  • 11
    • 36448991175 scopus 로고    scopus 로고
    • One-compartment model with Michaelis-Menten elimination kinetics and therapeutic window: an analytical approach
    • Tang S., Xiao Y. One-compartment model with Michaelis-Menten elimination kinetics and therapeutic window: an analytical approach. J. Pharmacokinet. Pharmacodyn. 2007, 34:807-827.
    • (2007) J. Pharmacokinet. Pharmacodyn. , vol.34 , pp. 807-827
    • Tang, S.1    Xiao, Y.2
  • 13
    • 77955841256 scopus 로고    scopus 로고
    • Analytical approximations to the solutions of the Michaelis-Menten equation
    • Mickens R.E., Hence C.R. Analytical approximations to the solutions of the Michaelis-Menten equation. Intl. J. Appl. Sci. Comput. 1998, 5:149-155.
    • (1998) Intl. J. Appl. Sci. Comput. , vol.5 , pp. 149-155
    • Mickens, R.E.1    Hence, C.R.2
  • 14
    • 0025944583 scopus 로고
    • Experimental designs for estimating the parameters of the Michaelis-Menten equation from progress curves of enzyme-catalyzed reactions
    • Duggleby R.G., Clarke R.B. Experimental designs for estimating the parameters of the Michaelis-Menten equation from progress curves of enzyme-catalyzed reactions. Biochim. Biophys. Acta 1991, 1080:231-236.
    • (1991) Biochim. Biophys. Acta , vol.1080 , pp. 231-236
    • Duggleby, R.G.1    Clarke, R.B.2
  • 15
    • 0029902679 scopus 로고    scopus 로고
    • Program DYNAFIT for the analysis of enzyme kinetic data: application to HIV proteinase
    • Kuzmic P. Program DYNAFIT for the analysis of enzyme kinetic data: application to HIV proteinase. Anal. Biochem. 1996, 237:260-273.
    • (1996) Anal. Biochem. , vol.237 , pp. 260-273
    • Kuzmic, P.1
  • 16
    • 33947318210 scopus 로고    scopus 로고
    • Full analytic progress curves of enzymatic reactions in vitro
    • Putz M.V., Lacrama A.M., Ostafe V. Full analytic progress curves of enzymatic reactions in vitro. Intl. J. Mol. Sci. 2006, 7:469-484.
    • (2006) Intl. J. Mol. Sci. , vol.7 , pp. 469-484
    • Putz, M.V.1    Lacrama, A.M.2    Ostafe, V.3
  • 18
    • 73849130978 scopus 로고    scopus 로고
    • Explicit solution of integrated 1-exp equation for predicting accumulation and decline of concentrations for drugs obeying nonlinear saturation kinetics
    • Keller F., Hartmann B., Czock D. Explicit solution of integrated 1-exp equation for predicting accumulation and decline of concentrations for drugs obeying nonlinear saturation kinetics. Ther. Drug Monit. 2009, 31:783-785.
    • (2009) Ther. Drug Monit. , vol.31 , pp. 783-785
    • Keller, F.1    Hartmann, B.2    Czock, D.3
  • 19
    • 28844444789 scopus 로고    scopus 로고
    • Uniform approximations for transcendental functions
    • Winitzki S. Uniform approximations for transcendental functions. Lecture Notes Comp. Sci. 2003, 2667:780-789.
    • (2003) Lecture Notes Comp. Sci. , vol.2667 , pp. 780-789
    • Winitzki, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.