Michael-Menten kinetics

Substrate (and product) profiles are obtained from the numerical resolution of the above differential equations (system of differential equations in the case of product inhibition). The corresponding local effectiveness factors (ratio of effective and intrinsic reaction rates) are then calculated and the global effectiveness factor determined from their profiles, as in the case of simple Michaels-Menten kinetics. Results are represented in three-dimensional plots in Figs. 4.15 to 4.18 respectively. 

Michaelis-Arbusov reaction, 19 29, 53, 54 Michaelis constant, 10 255 14 626-627 Michaelis-Menten equation, in kinetic studies, 14 625-627 Michaelis-Menten kinetics, 10 254-255 Michael reaction, 14 570 Michaels addition, of PVA, 25 602 Michelson interferometer, 14 221, 225 Micrinite, 6 707t... 

Kinetics of Model Substrates. In an effort to better understand enzymatic kinetics within reversed micelles, a-chymotrypsin hydrolysis of a model substrate, GPANA, was studied in CTAB reversed micelles. The hydrolysis kinetics of substrates by a-chymotrypsin is described by the Michaells-Menten formulation... 

The intrinsic ability of an organ to clear a drug is directly proportional to the activity of the metabolic enzymes in the organ. Such metabolic processes, both in vitro and in vivo, are characterized by Michael is-Menten kinetics ... 

Figure 6.4. Double-reciprocal plot for Michael is-Menten kinetics.

Michael-type acceptors 598 Michaelis-Menten kinetics 880 microwave-assisted organic synthesis (MAOS) 593... 

This prompted us to describe our kinetics for medium substrate concentrations also in terms of the Michael is-Menten scheme as Tsuchida et al. (2 0) did... 

Fig. 3 Michael s-Menten enzyme kinetics. Rate versus concentration profile for two competing substrates A and B, both showing simple saturation behavior. The kinetic domains are defined relative to the respective Michaelis constants that represent the substrate concentrations at which just one half of the maximal rate is reached.

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