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Tapan Dutta
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A new approach to a century-old problem: Henri-Michaelis-Menten enzyme kinetics
Mário Berberan-santos
AIP Conference Proceedings, 2012
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A note on the kinetics of enzyme action: A decomposition that highlights thermodynamic effects
Avi Flamholz
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An alternative analysis of enzyme systems based on the whole reaction time: evaluation of the kinetic parameters and initial enzyme concentration
Enrique Arribas
Journal of Mathematical Chemistry, 2007
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A general treatment of Henri–Michaelis–Menten enzyme kinetics: exact series solution and approximate analytical solutions
Mario Berberan e Santos
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Extending the kinetic solution of the classic Michaelis–Menten model of enzyme action
Volnei De Batista Carvalho
Journal of Mathematical Chemistry
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Enzyme kinetics - A modern approach
Jonathan Cisneros Pano
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The kinetics of an enzyme catalyzed reaction in the presence of an unstable, irreversible modifier
F. García-Cánovas
International Journal of Biochemistry, 1993
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Enzyme kinetics: the velocity of reactions
Antonio Baici
Biochemical Journal, 2006
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Metabolic control analysis in enzymes kinetics
MUSTAFA BAYRAM
2012
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On the Reducible Character of Haldane-Radić Enzyme Kinetics to Conventional and Logistic Michaelis-Menten Models
mihai putz
Molecules, 2011
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Michaelis-Menten Kinetics in Transient State: Proposal for Reversible Inhibition Model and its Application on Enzymatic Hydrolysis of Disaccharides
Lucas Oliveira
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The origins of enzyme kinetics
Cristina Hernandez
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Kinetic and Thermodynamic Aspects of Enzyme Control and Regulation †
Jan-Hendrik Hofmeyr, Johann Rohwer
The Journal of Physical Chemistry B, 2010
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Rate constants are determinable outside the original Michaelis–Menten mathematical formalism wherein the substrate concentration range is 1.6 4.8 times enzyme concentration: A pre-steady-state scenario and beyond
IKECHUKWU UDEMA
World Journal Of Advanced Research and Reviews, 2022
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IJERT-A Proposal for Reversible Enzymatic Inhibition Applied to the Michaelis-Menten Model in the Transient State
IJERT Journal
International Journal of Engineering Research and Technology (IJERT), 2016
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Chemical and enzyme kinetics
Kavi K
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Perturbation Theory in the Catalytic Rate Constant of the Henri–Michaelis–Menten Enzymatic Reaction
Evangelos Bakalis
Bulletin of Mathematical Biology, 2012
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Kinetic analysis of enzyme systems with suicide substrate in the presence of a reversible, uncompetitive inhibitor
F. García-Cánovas
Biosystems, 2001
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Enzyme Kinetics: Theory and Practice Reaction Rates and Reaction Order
Zifeng Song
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Rate constants are determinable outside the original Michaelis–Menten mathematical formalism wherein the substrate concentration range is approx. 1.6 to 4.8 times enzyme concentration: A pre-steady-state scenario and beyond
IKECHUKWU UDEMA
Zenodo (CERN European Organization for Nuclear Research), 2022
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17 Alternative Perspectives of Enzyme Kinetic Modeling
Ryan Walsh
2012
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Comparison of approximate kinetics for unireactant enzymes: Michaelis-Menten against the equivalent server
Alessio Angius
2010
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An analysis of the kinetics of unstable enzymatic systems using MAPLE
Necmettin Yildirim
Applied Mathematics and Computation, 2000
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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
F. García-Cánovas
Biochemical Journal, 1994
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Inhibition and Activation of Enzymes. The Effect of a Modifier on the Reaction Rate and on Kinetic Parameters
João Ribeiro
ACTA BIOCHIMICA POLONICA- …, 2000
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Substrate inhibition as a problem of non-linear steady state kinetics with monomeric enzymes
Peter Kaiser
Journal of Molecular Catalysis, 1980
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Kinetic behavior of membrane-bound, irreversible enzyme systems: experimental and theoretical considerations
Maithili Sharan
Journal of Histochemistry & Cytochemistry, 1982
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The Thermodynamic Description of Enzyme-Catalyzed Reactions
Hagai Rottenberg
Biophysical Journal, 1973
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