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Journal Abstract Search

195 related items for PubMed ID: 8003255

  • 1. Final phase of enzyme reactions following a Michaelis-Menten mechanisms in which the free enzyme and/or the enzyme-substrate complex are unstable.
    Varón R, Garrido del Solo C, García-Moreno M, Sánchez-Gracia A, García-Cánovas F.
    Biol Chem Hoppe Seyler; 1994 Jan; 375(1):35-42. PubMed ID: 8003255
    [Abstract] [Full Text] [Related]

  • 2. Kinetic analysis of a Michaelis-Menten mechanism in which the enzyme is unstable.
    Garrido-del Solo C, García-Cánovas F, Havsteen BH, Varón-Castellanos R.
    Biochem J; 1993 Sep 01; 294 ( Pt 2)(Pt 2):459-64. PubMed ID: 8373361
    [Abstract] [Full Text] [Related]

  • 3. Kinetics of inactivation of bovine pancreatic ribonuclease A by bromopyruvic acid.
    Wang MH, Wang ZX, Zhao KY.
    Biochem J; 1996 Nov 15; 320 ( Pt 1)(Pt 1):187-92. PubMed ID: 8947485
    [Abstract] [Full Text] [Related]

  • 4. An analysis of the kinetics of enzymatic systems with unstable species.
    Garrido-del Solo C, Havsteen BH, Varon R.
    Biosystems; 1996 Nov 15; 38(1):75-86. PubMed ID: 8833750
    [Abstract] [Full Text] [Related]

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  • 6. Validity of the Michaelis-Menten equation--steady-state or reactant stationary assumption: that is the question.
    Schnell S.
    FEBS J; 2014 Jan 15; 281(2):464-72. PubMed ID: 24245583
    [Abstract] [Full Text] [Related]

  • 7. Michaelis-Menten equation for degradation of insoluble substrate.
    Andersen M, Kari J, Borch K, Westh P.
    Math Biosci; 2018 Feb 15; 296():93-97. PubMed ID: 29197509
    [Abstract] [Full Text] [Related]

  • 8. Kinetic analysis of enzyme systems with suicide substrate in the presence of a reversible, uncompetitive inhibitor.
    Moruno-Dávila MA, Solo CG, García-Moreno M, García-Cánovas F, Varón R.
    Biosystems; 2001 Jun 15; 61(1):5-14. PubMed ID: 11448521
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  • 10. The kinetic effect of product instability in a Michaelis-Menten mechanism with competitive inhibition.
    Garrido-del Solo C, Moruno MA, Havsteen BH, Castellanos RV.
    Biosystems; 2000 Jun 15; 56(2-3):75-82. PubMed ID: 10880856
    [Abstract] [Full Text] [Related]

  • 11. Kinetics of an enzyme reaction in which both the enzyme-substrate complex and the product are unstable or only the product is unstable.
    Garrido-del Solo C, García-Cánovas F, Havsteen BH, Valero E, Varón R.
    Biochem J; 1994 Oct 15; 303 ( Pt 2)(Pt 2):435-40. PubMed ID: 7980401
    [Abstract] [Full Text] [Related]

  • 12. A Kinetic Analysis of Coupled (or Auxiliary) Enzyme Reactions.
    Eilertsen J, Schnell S.
    Bull Math Biol; 2018 Dec 15; 80(12):3154-3183. PubMed ID: 30288641
    [Abstract] [Full Text] [Related]

  • 13. Exact and approximate solutions for the decades-old Michaelis-Menten equation: Progress-curve analysis through integrated rate equations.
    Goličnik M.
    Biochem Mol Biol Educ; 2011 Dec 15; 39(2):117-25. PubMed ID: 21445903
    [Abstract] [Full Text] [Related]

  • 14. Sigmoidal substrate saturation curves in Michaelis-Menten mechanism as an artefact.
    Fischer E, Keleti T.
    Acta Biochim Biophys Acad Sci Hung; 1975 Dec 15; 10(3):221-7. PubMed ID: 1211106
    [Abstract] [Full Text] [Related]

  • 15. Theory on the rate equations of Michaelis-Menten type enzyme kinetics with competitive inhibition.
    Murugan R.
    PLoS One; 2024 Dec 15; 19(7):e0302679. PubMed ID: 39024204
    [Abstract] [Full Text] [Related]

  • 16. About and beyond the Henri-Michaelis-Menten rate equation for single-substrate enzyme kinetics.
    Bajzer Z, Strehler EE.
    Biochem Biophys Res Commun; 2012 Jan 20; 417(3):982-5. PubMed ID: 22206668
    [Abstract] [Full Text] [Related]

  • 17. Dynamic disorder in single-molecule Michaelis-Menten kinetics: the reaction-diffusion formalism in the Wilemski-Fixman approximation.
    Chaudhury S, Cherayil BJ.
    J Chem Phys; 2007 Sep 14; 127(10):105103. PubMed ID: 17867782
    [Abstract] [Full Text] [Related]

  • 18. The steady-state Michaelis-Menten analysis of P-glycoprotein mediated transport through a confluent cell monolayer cannot predict the correct Michaelis constant Km.
    Bentz J, Tran TT, Polli JW, Ayrton A, Ellens H.
    Pharm Res; 2005 Oct 14; 22(10):1667-77. PubMed ID: 16180124
    [Abstract] [Full Text] [Related]

  • 19. A method to describe enzyme-catalyzed reactions by combining steady state and time course enzyme kinetic parameters.
    Walsh R, Martin E, Darvesh S.
    Biochim Biophys Acta; 2010 Jan 14; 1800(1):1-5. PubMed ID: 19840832
    [Abstract] [Full Text] [Related]

  • 20. Comparison of conformational changes and inactivation of soybean lipoxygenase-1 during urea denaturation.
    Wu Y, Wang ZX.
    Biochim Biophys Acta; 1998 Nov 10; 1388(2):325-36. PubMed ID: 9858760
    [Abstract] [Full Text] [Related]

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