9. Describe the ping-pong mechanism using Lineweaver-Burk plot? (5pts)
What is one major disadvantage of using a Lineweaver-Burk plot for determination of kinetic parameters from real data? A.) A Lineweaver-Burk plot biases data with fast initial velocities B.) The Lineweaver-Burk plots tend to be reliant on how reproducible the initial rate is C.) The Lineweaver-Burk plot biases low concentration data D.) all of the above
What is one major disadvantage of using a Lineweaver-Burk plot for determination of kinetic parameters from real data? A.) A Lineweaver-Burk plot biases data with fast initial velocities B.) The Lineweaver-Burk plots tend to be reliant on how reproducible the initial rate is C.) The Lineweaver-Burk plot biases low concentration data D.) all of the above
1. Why must the maximum velocity (Vmax) be determined using a Lineweaver-Burk plot and not the MichaelisMenten Plot?
how do you create a Michealis-Menten plot and a Lineweaver- Burk plot using the equation that is determine from a calibration curve of absorbance vs. time? How do you convert the absorbance determine into concentration?
Examine the formula for the kinetics of a ping-pong bisubstrate reaction, 1/v = (KmA / Vmax)(1/[A]) + (1 + KmB/[B])(1/Vmax) Show that for high concentrations of [B], particularly [B] >> KmB, this equation reduces to the ordinary Lineweaver-Burk formula for the other substrate, A.
If a Lineweaver-Burk plot gives a line with an equation of y = 0.33 x + 0.55, what are the values of KM and Vmax?
describe the ping pong method of facilitated diffusion
For a report, after plotting the lineweaver-burk plot for a protease enzyme with and without inhibitor. It shows that the km value increases in the presence of inhibitor and Vmax decreases. what type of inhibition is it? The inhibitor is an azide.
Write the equations that describe the Michaelis-Menten and the Lineweaver-Burk double-reciprocal plots. Draw examples of each plot, demonstrating how Km and Vmax can be determined. On the same graphs, draw another plot where the same enzyme-catalyzed reaction is subjected to inhibition by a competitive inhibitor.
LINEWEAVER-BURK plot 1. You perform the hydrolysis reaction as required in the lab experiment, and the final reading on your blood glucose meter for one of your samples is 385 mg/dL. You need your data to be in units of mm (millimolar, which is millimoles per liter, abbreviated as mmol/L). Show, in a step-by-step conversion, how you would convert 385 mg/dL to the proper answer in mM. 385 mg dlº= ?mm immoles 2. Assuming that the reaction occurred over a...