[8] Kinetic analysis of progress curves
References (27)
- et al.
Biochim. Biophys. Acta
(1964) Arch. Biochem. Biophys.
(1963)- et al.
Biochim. Biophys. Acta
(1978) J. Biol. Chem.
(1969)- et al.
Biochim. Biophys. Acta
(1977) Principles of Enzyme Kinetics
C. R. Acad. Sci.
(1902)- et al.
Arch. Biochem. Biophys.
(1944) - et al.
- et al.
The Chemical Kinetics of Enzyme Action
(1973)
J. Am. Chem. Soc.
J. Am. Chem. Soc.
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2021, Journal of Molecular BiologyCitation Excerpt :Unsuspected interferences such as those caused by enzyme inactivation and inhibition are known to have major effects on the reproducibility of kinetic results [10,11]. These effects can substantially accumulate over time, thereby affecting the determination of kinetic parameters by full time-course analysis [12,13]. Also, classical initial velocity analysis can heavily depend on subjective selection criteria, especially under conditions of low substrate concentration for which the “initial linear phase” is not easily observable [14].
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2019, Biophysical ChemistryCitation Excerpt :The reactions were initiated by the addition of α-thrombin and followed at 405 nm using a Synergy2 multi-mode microplate reader (BioTek Winooski, USA) [27]. The main differences of this formalism relatively to Eq. (1) are: (a) the use of apparent kinetic constants Kmapp and Vapp, (b) the use of partial time intervals (∆t = t − ti) and of the corresponding increment of product concentration (∆P = P − Pi), (c) the initial condition (subscript i) is now any point of the reaction subsequent to the pre-steady-state phase (ti > t∗), (d) the final concentration of product is given by the measured value (P∞) and not by the expected value (S0) [30], and (e) Eq. (2) is presented in a linearized form of the Walker and Schmidt type [35] (Fig. 2b). Features (a) to (c) are meant to expand the validity of time-course analysis to the same range of conditions of the steady-state assumption (E0 ≪ S0 + Km) [34,36].
Enzyme inhibition studies by integrated Michaelis-Menten equation considering simultaneous presence of two inhibitors when one of them is a reaction product
2016, Computer Methods and Programs in BiomedicineConstitutive phosphorylation of cardiac myosin regulatory light chain in vivo
2015, Journal of Biological ChemistryCitation Excerpt :Non-linear regression of the time course of RLC phosphorylation showed a monophasic reaction with no evidence of negative cooperativity (data not shown). Linearization of the reaction, as described previously (44–46), illustrates the monophasic process, indicating that the phosphorylation reaction was kinetically homogeneous (Fig. 5). If half of the RLCs were phosphorylated at a slower rate, the regression would not be monophasic.
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