The hydrolysis of sucrose by the enzyme invertase was followed by measuring the initial rate of change in polarimeter (optical rotation) readings, a, at various initial concentrations of sucrose. The reaction is inhibited reversibly by the addition of urea:
[Sucrose] o, mol L-1 | 0.0292 0.0584 0.0876 | 0.117 | 0.175 | 0.234 | ||
Initial rate, (da/dt)0 = V0 | 0.182 | 0.265 | 0.311 | 0.330 | 0.372 | 0.371 |
Initial rate (2 M urea), V0' | 0.083 | 0.119 | 0.154 | 0.167 | 0.192 | 0.188 |
a. Make a plot of the data in the absence of urea and determine the Michaelis constant KM for this reaction.
b. Carry out an analysis of the data in the presence of urea and determine whether urea is a competitive or a noncompetitive inhibitor of the enzyme for this reaction. Justify your answer
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