Virtual Investigation of an Enzyme. A new protease (ref. no PR/66-430-010), isolated from B.yorkii has been characterised. A series of experiments were run on the enzyme to determine the optimum pH for the enzyme to run at, the effect of pH on KM and Vmax
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Introduction
Summary I. A new protease (ref. no PR/66-430-010), isolated from B.yorkii has been characterised. II. A series of experiments were run on the enzyme to determine the optimum pH for the enzyme to run at, the effect of pH on KM and Vmax, to determine the effect of azide on substrate binding, on the catalytic process itself or both and also to determine the dissociation constant for the enzyme-azide complex and the accuracy of the measurements. III. Experiments performed on the isolated enzyme showed that if the pH of the solution was too high then the rate of reaction is too slow to gain any results and the same was true if the ph is too low. ...read more.
Middle
Control Vmax - 1/0.35 = 2.9 Km - 1/15 = 0.06 Inhibitor Vmax - 1/0.35 = 2.9 Km - 1/4 = 0.25 Double Inhibitor Vmax - 1/0.35 = 2.9 Km - 1/2.5 = 0.4 Discussion The precision of the assay procedure was determined using the following data: Vol �mol pH S �mol I �mol V 10 7 0.06 0 1.1567 10 7 0.06 0 1.2057 10 7 0.06 0 1.2121 10 7 0.06 0 1.2698 10 7 0.06 0 1.145 mean 1.19075 SD= 0.047842439 The mean of the velocity was calculated as 1.19075 and the standard deviation (SD) was calculated to be 0.047842439. The effect of pH on the enzyme was determined when the following results were obtained and then plotted as in Fig. ...read more.
Conclusion
The same was true for the velocity when the pH was lowered, with the velocity again dropping. The effect of the inhibitor azide can be seen from Fig.2 to slow the velocity and reduce the Km of the reaction. When the concentration of azide was at 0.2�mol the inhibition was at it's highest and when the concentration of the inhibitor was doubled, the inhibition rate was reduced slightly. Also, from the Lineweaver-Burk plot is was determined that azide is a competitive inhibitor. This was determined because the lines of best fit of the solutions which contained the inhibitor crossed at the same point on the y-axis and met with the control experiment at this point. Biol 201 Workshop - A Virtual Investigation Of An Enzyme Sean Lenahan ...read more.
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