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Journal Abstract Search

205 related items for PubMed ID: 2246902

  • 21.
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  • 22. The general modifier ("allosteric") unireactant enzyme mechanism: redundant conditions for reduction of the steady state velocity equation to one that is first degree in substrate and effector.
    Segel IH, Martin RL.
    J Theor Biol; 1988 Dec 19; 135(4):445-53. PubMed ID: 3256732
    [Abstract] [Full Text] [Related]

  • 23. [Stationary kinetics of multisubstrate enzymatic reactions. Inhibition by reaction products, reversible and irreversible inhibitors].
    Vrzheshch PV.
    Biokhimiia; 1988 Oct 19; 53(10):1704-11. PubMed ID: 3233227
    [Abstract] [Full Text] [Related]

  • 24. Why do many Michaelian enzymes exhibit an equilibrium constant close to unity for the interconversion of enzyme-bound substrate and product?
    Pettersson G.
    Eur J Biochem; 1991 Feb 14; 195(3):663-70. PubMed ID: 1999189
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  • 28. 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
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  • 29. Evolutionary optimization of the catalytic efficiency of enzymes.
    Pettersson G.
    Eur J Biochem; 1992 May 15; 206(1):289-95. PubMed ID: 1587280
    [Abstract] [Full Text] [Related]

  • 30. Modelling of chemical reactions catalysed by membrane-bound enzymes. Determination and significance of the kinetic constants.
    Heirwegh KP, Meuwissen JA, Van den Steen P, De Smedt H.
    Biochim Biophys Acta; 1989 Apr 06; 995(2):151-9. PubMed ID: 2930793
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  • 31.
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  • 32. Experimental approach to the kinetic study of unstable site-directed irreversible inhibitors: kinetic origin of the apparent positive co-operativity arising from inactivation of trypsin by p-amidinophenylmethanesulphonyl fluoride.
    Espín JC, Tudela J.
    Biochem J; 1994 Apr 01; 299 ( Pt 1)(Pt 1):29-35. PubMed ID: 8166652
    [Abstract] [Full Text] [Related]

  • 33. Isomerization of the free enzyme versus induced fit: effects of steps involving induced fit that bypass enzyme isomerization on flux ratios and countertransport.
    Britton HG.
    Biochem J; 1997 Jan 01; 321 ( Pt 1)(Pt 1):187-99. PubMed ID: 9003418
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  • 34. Kinetic analysis of modification reactions at comparable enzyme and modifier concentrations.
    Zhao KY, Wang ZX.
    J Theor Biol; 1996 Aug 21; 181(4):319-27. PubMed ID: 8949580
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  • 38. [Qualitative analysis of a mathematical model of a open enzyme reaction].
    Kaĭmachnikov NP.
    Biofizika; 1978 Aug 21; 23(2):247-52. PubMed ID: 647034
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  • 40. Analysis of progress curves for a highly concentrated Michaelian enzyme in the presence or absence of product inhibition.
    Kellershohn N, Laurent M.
    Biochem J; 1985 Oct 01; 231(1):65-74. PubMed ID: 4062893
    [Abstract] [Full Text] [Related]

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