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A Windows program for the derivation of steady-state equations in enzyme systems

Applied mathematics and computation, 2006-10, Vol.181 (2), p.837-852

2006

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The kinetic effect of the inactivation of the enzyme–substrate complex in an enzymatic reaction with slow-binding inhibition

Applied mathematics and computation, 2005-12, Vol.171 (1), p.450-463

2005

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A COMPARISON BETWEEN THE INITIAL RATE EXPRESSIONS OBTAINED UNDER STRICT CONDITIONS AND THE RAPID EQUILIBRIUM ASSUMPTION USING, AS EXAMPLE, A FOUR SUBSTRATE ENZYME REACTION

Journal of theoretical & computational chemistry, 2011-10, Vol.10 (5), p.659-678

2011

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The influence of product instability on slow-binding inhibition

Journal of enzyme inhibition and medicinal chemistry, 2005-08, Vol.20 (4), p.309-316

2005

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Kinetic analysis of enzyme systems with suicide substrate in the presence of a reversible competitive inhibitor, tested by simulated progress curves

The international journal of biochemistry & cell biology, 2001-02, Vol.33 (2), p.181-191

2001

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Kinetic Analysis of the General Modifier Mechanism of Botts and Morales Involving a Suicide Substrate

Journal of theoretical biology, 2002-10, Vol.218 (3), p.355-374

2002

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Transient phase of enzyme reactions.: Time course equations of the strict and the rapid equilibrium conditions and their computerized derivation

BioSystems, 1999-05, Vol.50 (2), p.99-126

1999

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Kinetic analysis of enzyme systems with suicide substrate in the presence of a reversible, uncompetitive inhibitor

BioSystems, 2001-06, Vol.61 (1), p.5-14

2001

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Kinetics of an enzyme reaction in which both the enzyme-substrate complex and the product are unstable or only the product is unstable

Biochemical journal, 1994-10, Vol.303 ( Pt 2) (2), p.435-440

1994

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Kinetic analysis of a Michaelis-Menten mechanism in which the enzyme is unstable

Biochemical journal, 1993-09, Vol.294 ( Pt 2) (2), p.459-464

1993

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An analysis of the kinetics of enzymatic systems with unstable species

BioSystems, 1996, Vol.38 (1), p.75-86

1996

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Kinetics of enzyme systems with unstable suicide substrates

BioSystems, 1998-08, Vol.47 (3), p.177-192

1998

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Use of a windows program for simulation of the progress curves of reactants and intermediates involved in enzyme-catalyzed reactions

BioSystems, 2000, Vol.54 (3), p.151-164

2000

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Kinetic analysis of enzyme reactions with slow-binding inhibition

BioSystems, 1999-09, Vol.51 (3), p.169-180

1999

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The kinetic effect of product instability in a Michaelis–Menten mechanism with competitive inhibition

BioSystems, 2000-04, Vol.56 (2), p.75-82

2000

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Kinetic analysis of a Michaelis—Menten mechanism with an unstable substrate

Journal of molecular catalysis, 1993-07, Vol.83 (1), p.273-285

1993

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The kinetics of an enzyme catalyzed reaction in the presence of an unstable, irreversible modifier

International journal of biochemistry, 1993, Vol.25 (12), p.1889-1895

1993

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Analysis of progress curves of enzymatic reactions with unstable species

The international journal of biochemistry & cell biology, 1996-12, Vol.28 (12), p.1371-1379

1996

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Transient phase of enzyme reactions

BioSystems, 1999-05, Vol.50 (2), p.99-126

1999

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The influence of product instability on Michaelis-Menten kinetics under steady-state and rapid equilibrium assumptions

The international journal of biochemistry & cell biology, 1995-05, Vol.27 (5), p.475-479

1995

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Kinetic analysis of a Michaelis-Menten mechanism in which the enzyme is instable

Biochemical journal, 1993, Vol.294, p.459-464

1993

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Final phase of enzyme reactions following a Michaelis-Menten mechanisms in which the free enzyme and/or the enzyme-substrate complex are unstable

Biological chemistry Hoppe-Seyler, 1994-01, Vol.375 (1), p.35

1994

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Kinetic analysis of the michaelis-menten mechanism in which the substrate and the product are unstable

International journal of biochemistry, 1994-05, Vol.26 (5), p.645-651

1994

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A Windows program for the derivation of steady-state equations in enzyme systems

The kinetic effect of the inactivation of the enzyme–substrate complex in an enzymatic reaction with slow-binding inhibition

A COMPARISON BETWEEN THE INITIAL RATE EXPRESSIONS OBTAINED UNDER STRICT CONDITIONS AND THE RAPID EQUILIBRIUM ASSUMPTION USING, AS EXAMPLE, A FOUR SUBSTRATE ENZYME REACTION

The influence of product instability on slow-binding inhibition

Kinetic analysis of enzyme systems with suicide substrate in the presence of a reversible competitive inhibitor, tested by simulated progress curves

Kinetic Analysis of the General Modifier Mechanism of Botts and Morales Involving a Suicide Substrate

Transient phase of enzyme reactions.: Time course equations of the strict and the rapid equilibrium conditions and their computerized derivation

Kinetic analysis of enzyme systems with suicide substrate in the presence of a reversible, uncompetitive inhibitor

Kinetics of an enzyme reaction in which both the enzyme-substrate complex and the product are unstable or only the product is unstable

Kinetic analysis of a Michaelis-Menten mechanism in which the enzyme is unstable

An analysis of the kinetics of enzymatic systems with unstable species

Kinetics of enzyme systems with unstable suicide substrates

Use of a windows program for simulation of the progress curves of reactants and intermediates involved in enzyme-catalyzed reactions

Kinetic analysis of enzyme reactions with slow-binding inhibition

The kinetic effect of product instability in a Michaelis–Menten mechanism with competitive inhibition

Kinetic analysis of a Michaelis—Menten mechanism with an unstable substrate

The kinetics of an enzyme catalyzed reaction in the presence of an unstable, irreversible modifier

Analysis of progress curves of enzymatic reactions with unstable species

Transient phase of enzyme reactions

The influence of product instability on Michaelis-Menten kinetics under steady-state and rapid equilibrium assumptions

Kinetic analysis of a Michaelis-Menten mechanism in which the enzyme is instable

Final phase of enzyme reactions following a Michaelis-Menten mechanisms in which the free enzyme and/or the enzyme-substrate complex are unstable

Kinetic analysis of the michaelis-menten mechanism in which the substrate and the product are unstable

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