3. Show that the inverse of equation 29-78 in the textbook gives the Lineweaver-Burk Equation. The hydration of CO2 is catalyzed by the enzyme carbonic anhydrase. For a total enzyme concentration of 2.32 x 10-⁹ M, the following data were obtained. [CO2]o (M) 0.00125 0.00250 0.00500 0.02000 v (M/s) 2.78 x 10-5 5.00 x 10-5 8.33 x 10-5 1.66 x 10-4 Plot these according to the Burke-Lineweaver Equation and determine the values of Km, the Michaelis constant, and k2, the rate constant for product formation from the enzyme-substrate complex from the slope and intercept of the plotted data.

Principles Of Pharmacology Med Assist
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ISBN:9781337512442
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Chapter1: Numerals And Fractions
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3. Show that the inverse of equation 29-78 in the textbook gives the Lineweaver-Burk
Equation.
The hydration of CO2 is catalyzed by the enzyme carbonic anhydrase. For a total enzyme
concentration of 2.32 x 10-⁹M, the following data were obtained.
[CO2]o (M) v (M/s)
0.00125
2.78 x 10-5
0.00250
5.00 x 10-5
0.00500
8.33 x 10-5
0.02000 1.66 x 10-4
Plot these according to the Burke-Lineweaver Equation and determine the values of Km, the
Michaelis constant, and k2, the rate constant for product formation from the enzyme-substrate
complex from the slope and intercept of the plotted data.
Transcribed Image Text:3. Show that the inverse of equation 29-78 in the textbook gives the Lineweaver-Burk Equation. The hydration of CO2 is catalyzed by the enzyme carbonic anhydrase. For a total enzyme concentration of 2.32 x 10-⁹M, the following data were obtained. [CO2]o (M) v (M/s) 0.00125 2.78 x 10-5 0.00250 5.00 x 10-5 0.00500 8.33 x 10-5 0.02000 1.66 x 10-4 Plot these according to the Burke-Lineweaver Equation and determine the values of Km, the Michaelis constant, and k2, the rate constant for product formation from the enzyme-substrate complex from the slope and intercept of the plotted data.
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