Essay on A Report On Michaelis Menten Kinetics
Nelson et al, 2008, state “all enzymes that exhibit a hyperbolic dependence of V0 on [S] are said to follow Michaelis-Menten kinetics”. The data gathered from this experiment and plotted in figure 6 shows that it is this pattern shown in the reaction of PNPP to PNP catalysed by acid phosphatase, where a hyperbolic curve is observed in the graph of rate of reaction against substrate concentration, approaching the Vmax asymptotically. Acid phosphatase behaved congruently to the Michaelis-Menten model.
Vmax was determined as 6.65 x 10-3 µmol/min using the Lineweaver-Burk plot. However, as was highlighted in the results, one of the experimental data points produced a rate of reaction of 6.89 x 10-3 µmol/min – greater than that of the maximum expected. It can be seen in figure 7 that, while there is certainly a strong linear correlation giving a coefficient of determination of 0.9733, several of the data points, particularly those at higher concentrations, fell away from the trendline. This may have caused the trendline to be skewed. Alternatively, the data point itself may have been subject to experimental error.
In this experiment, the Lineweaver-Burk derived value of Vmax has not been used for any further calculations. However, if the data were to be expanded on further (for example, in the calculation of Kcat) this could exacerbate the potential error. Further repeats of the experiment would have been advisable in regards to this.
In addition, Frey and Hegeman…