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The plot is occasionally attributed to Augustinsson [5] and referred to the Woolf–Augustinsson–Hofstee plot [6] [7] [8] or simply the Augustinsson plot. [9] However, although Haldane, Woolf or Eadie were not explicitly cited when Augustinsson introduced the versus / equation, both the work of Haldane [10] and of Eadie [3] are cited at other places of his work and are listed in his ...
The best known plots of the Michaelis–Menten equation, including the double-reciprocal plot of / against /, [2] the Hanes plot of / against , [3] and the Eadie–Hofstee plot [4] [5] of against / are all plots in observation space, with each observation represented by a point, and the parameters determined from the slope and intercepts of the lines that result.
The Lineweaver–Burk plot derives from a transformation of the Michaelis–Menten equation, v = V a K m + a {\displaystyle v={\frac {Va}{K_{\mathrm {m} }+a}}} in which the rate v {\displaystyle v} is a function of the substrate concentration a {\displaystyle a} and two parameters V {\displaystyle V} , the limiting rate , and K m {\displaystyle ...
Enzymes are proteins that act as biological catalysts by accelerating chemical reactions. Enzymes act on small molecules called substrates, which an enzyme converts into products. Almost all metabolic processes in the cell need enzyme catalysis in order to occur at rates fast enough to sustain life.
Determining the parameters of the Michaelis–Menten equation typically involves running a series of enzyme assays at varying substrate concentrations , and measuring the initial reaction rates , i.e. the reaction rates are measured after a time period short enough for it to be assumed that the enzyme-substrate complex has formed, but that the ...
Like other techniques that linearize the Michaelis–Menten equation, the Hanes–Woolf plot was used historically for rapid determination of the kinetic parameters , and /, but it has been largely superseded by nonlinear regression methods that are significantly more accurate and no longer computationally inaccessible. It remains useful ...
A calibration curve plot showing limit of detection (LOD), limit of quantification (LOQ), dynamic range, and limit of linearity (LOL).. In analytical chemistry, a calibration curve, also known as a standard curve, is a general method for determining the concentration of a substance in an unknown sample by comparing the unknown to a set of standard samples of known concentration. [1]
A comparison of specificity constants can also be used as a measure of the preference of an enzyme for different substrates (i.e., substrate specificity). The higher the specificity constant, the more the enzyme "prefers" that substrate. [1] The following equation, known as the Michaelis–Menten model, is used to describe the kinetics of enzymes: