1. Why must the maximum velocity (Vmax) be determined using a Lineweaver-Burk plot and not the MichaelisMenten Plot?
1. Why must the maximum velocity (Vmax) be determined using a Lineweaver-Burk plot and not the...
Name Page Number Date Vmax 1. Estimate Vmax and Km using the velocity vs. substrate concentration plot - KM 2. Calculate the Vmax and Km using the Lineweaver-Burk plot. KM Vmax (S), uM 0.08 0.12 0.54 1.23 1.82 2.72 Reaction Velocity (UM/min) 0.15 0.21 0.70 1.1 1.3 15 4.94 10.00 1.8
How can the Michaelis-Menten constant, be derived from this Lineweaver-Burk plot? Vmax O km = (-1)/(x-intercept) O km = (-1) * (x-intercept) O km = 1/(x-intercept) 0 Km = s;lope
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?
12. From the Lineweaver-Burk graph given: a. What are the Km and Vmax for the uninhibited case? b. What type of inhibition is occurring? c. Shown on the page after the Lineweaver-Burk plot are semi-qualitative sketches for three V vs. (S) plots. Which one of these most likely corresponds to this particular experiment (A,B or C)? Scani explain th Cant catimer IIIIIIIII IIIIIIIII - -- | - | IIIII We were unable to transcribe this image
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
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.
how do you make a lineweaver-burk plot where the trend line extends backwards? is there a way of figuring out how far back it should extend based of your data ? As well, how do you plot two sets of data on one graph ? Thank you! (idk if you need to see my data-> attached below) Biochemistry Enzyme Kinetics Assignment Four answers for this assignment will be completed in elearn: En in elearn: Enzyme Kinetics Quiz ots but must...
9. Describe the ping-pong mechanism using Lineweaver-Burk plot? (5pts)
(I need help with part C, Drawing the expected Michaelis-Menten plot; Do NOT draw the Lineweaver-Burk plot. thanks!) 1. Michaelis-Menten kinetics- use the M-M equation to answer the following: a. An enzyme (5 µM) has a Vmax of 450 mM/min. What is kcat? b. When the substrate concentration is 50 mM, the initial velocity (V0) was measured to be 375 mM/min. Under the conditions described above, calculate the KM. c. Draw the expected Michaelis-Menten plot (label your axes and include...