Q10.11 (a) For the given data, the Lineweaver Burk plot gives a straight line. Hence, this reaction follows Michaelis-Menten kinetics.
(b) The equation of straight line is : y = 0.5013x + 6234.3
slope = 0.5013 min
intercept = 6234.3 min/M
Vmax = 1/intercept
Vmax = 1/(6234.3 min/M)
Vmax = 1.604 x 10-4 M/min
Vmax = 160.4 x 10-6 M/min
(c) Km = (slope) / (intercept)
Km = (0.5013 min) / (6234.3 min/M)
Km = 8.04 x 10-5 M
10.11 The initial rates at various substra tions for an enzyme-catalyzed reaction are ious substrate concentra...
7. a) In an enzyme catalyzed reaction which follows the Michaelis-Menten kinetics. The substrate concentration (Km, Michaelis constant) needed to reach 50% of the maximum reaction velocity (Vmax) is 20 μΜ. What substrate concentration is required to obtain at least 75% of the maximum reaction velocity? Show the work to get full points. (5 points) b) You want to load 10 μg of protein in 15 μL into one of the 10% polyacrylamide gel well. The protein needs to be...
s- (3 pts) The flowing rates have been an enzyme- catalyzed reaction at various substrate concentrations: Run no. 103 [S]M Rate, v/ (Ms') 2.41 3.33 4.78 6.17 7.41 9.52 0.0 12.5 0.4 0.6 4 2.0 4.0 a- From Line-Weaver double reciprocal plot, obtain and Mechaelis-Menten constant, max b- If the enzyme concentration is 1.00 x 10-11 M calculate kz.
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