Assuming the in vitro conditions for the enzyme-catalyzed reactions, the basic Michaelis-Menten description is modified in a logistic (mathematical) manner such that the inherent limitations that appear in the previous method are removed. Beside its generality, the reliability of the present approach is proved through applications on the competitive multi- and bi- substrate enzyme catalyses
The nature and validity of the mathematical formulation of Michaelis-Menten type kinetics for enzyme...
A simple thermodynamic analysis of the well-known Michaelis-Menten equation (MME) of enzyme catalysi...
Mathematical models, especially when coupled with modern computer techniques, prove to be very effec...
Assuming the in vitro conditions for the enzyme-catalyzed reactions, the basic Michaelis-Menten desc...
Accurate measurement of the quantitative aspects of enzyme-catalysed reactions is critical for a dee...
The principal aim of studies of enzyme-mediated reactions has been to provide comparative and quanti...
The principal aim of studies of enzyme-mediated reactions has been to provide comparative and quanti...
Schleeger M, Heberle J, Kakorin S. Assessment of Michaelis-Menten parameters by analysis of single t...
© 2019 Elsevier B.V. Progress curves for competing substrates were analyzed to investigate the effec...
© 2019 Elsevier B.V. Progress curves for competing substrates were analyzed to investigate the effec...
The aim of the research is to analize and model the progress of product accumulation in relation wit...
There are several advantages to the use of progress curves to analyze the kinetic properties of enzy...
When the progress curve for an enzyme catalyzed reaction follows the integrated Michaelis-Menten equ...
Progress curves of enzyme-catalysed reactions are described by equations of a type that precludes di...
The nature and validity of the mathematical formulation of Michaelis-Menten type kinetics for enzyme...
The nature and validity of the mathematical formulation of Michaelis-Menten type kinetics for enzyme...
A simple thermodynamic analysis of the well-known Michaelis-Menten equation (MME) of enzyme catalysi...
Mathematical models, especially when coupled with modern computer techniques, prove to be very effec...
Assuming the in vitro conditions for the enzyme-catalyzed reactions, the basic Michaelis-Menten desc...
Accurate measurement of the quantitative aspects of enzyme-catalysed reactions is critical for a dee...
The principal aim of studies of enzyme-mediated reactions has been to provide comparative and quanti...
The principal aim of studies of enzyme-mediated reactions has been to provide comparative and quanti...
Schleeger M, Heberle J, Kakorin S. Assessment of Michaelis-Menten parameters by analysis of single t...
© 2019 Elsevier B.V. Progress curves for competing substrates were analyzed to investigate the effec...
© 2019 Elsevier B.V. Progress curves for competing substrates were analyzed to investigate the effec...
The aim of the research is to analize and model the progress of product accumulation in relation wit...
There are several advantages to the use of progress curves to analyze the kinetic properties of enzy...
When the progress curve for an enzyme catalyzed reaction follows the integrated Michaelis-Menten equ...
Progress curves of enzyme-catalysed reactions are described by equations of a type that precludes di...
The nature and validity of the mathematical formulation of Michaelis-Menten type kinetics for enzyme...
The nature and validity of the mathematical formulation of Michaelis-Menten type kinetics for enzyme...
A simple thermodynamic analysis of the well-known Michaelis-Menten equation (MME) of enzyme catalysi...
Mathematical models, especially when coupled with modern computer techniques, prove to be very effec...
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