How does the slope of a Lineweaver-Burk line influence initial velocity? A. Increases initial velocity B. Decreases initial velocity C. Does not impact initial velocity, only substrate concentration does D. Only Vmax impacts initial reaction velocity 1/Vo Slope = KM/Vmax 1 Intercept = -1/KM Intercept 1/Vmax = Км 1 = νο + Vmax [S] Vmax y = slope x + intercept 1/[S]
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![How does the slope of a Lineweaver-Burk line influence initial velocity?
A. Increases initial velocity
B. Decreases initial velocity
C. Does not impact initial velocity, only substrate concentration does
D. Only Vmax impacts initial reaction velocity
1/Vo Slope = KM/Vmax
1
Intercept = -1/KM
Intercept 1/Vmax
=
Км 1
=
νο
+
Vmax [S] Vmax
y = slope x + intercept
1/[S]](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F2721ccf2-fbe1-4868-87fa-588e33d78a8e%2Fb238bb6d-d5e8-4a90-b4ac-488643a34809%2Fbw2ulyy_processed.png&w=3840&q=75)
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- How does one measure Km using a Lineweaver-Burk plot? 1. By determining the reciprocal of the y-intercept 2. By determining the negative reciprocal of the x-intercept 3. By determining the slope and multiplying it by kcat 4. By determining the saturation pointA. Kinetics Data 1/[S], mM- 0.5714 0.4608 0.3333 0.1818 0.0952 1/Velocity (min/mM) Inhibited 0.7246 0.5988 0.4694 0.3367 0.26109 Uninhibited 0.5154 0.4424 0.3508 0.2816 0.2277 B. Lineweaver-Burk Plot and Analysis Paste your Microsoft Excel Graph of the kinetic analysis. Compute for Vmax and Km values and identify the mode of enzyme inhibition involved.A forest rich in eucalyptus trees grows well after fıres that clear the competing undergrowth, assuming that other conditions are good. Therefore, they have O low facilitation high facilitation low resilience high inertia O low inertia
- For a gradient system with a gradient of 5-90% in 50 min, flow 2 mL/min, column 100 x 4.6 mm i.d., the first peak elutes at 20 min, and the last peak elutes at 50 min. Calculate k* for this system. 2. Can isocratic elution be used for this sample? If so, what is the range of k values to be expected. 3.Propose a way to shorten the gradient run time by eliminating the wait for the first peak to elute at 20 min. 4. For the original conditions of this question, change the conditions necessary to use a 150 x 4.6 mm column while maintaining the same k* value.Which of the following changes goes along with a decreased clearance and no change in volume of distribution? Please select one: a. shorter half-life, higher steady state concentration b. Increased initial concentration after an i.v. bolus, longer time to steady state c. Longer time to steady state, higher steady state concentration d. Longer time to steady state, lower steady state concentration e. longer time to steady state, shorter half-lifeUsing the Michaelis-Mentan graph pictured (graphing initial velocity and PNPP concentration), identify Vmax and Km as well as possible. Then, using the Lineweaver-Burk graph (graphing 1/Vo and 1 / PNPP concentration), label the reciprocals of Vmax and Km on the graph and use them to calculate Km and Vmax.
- Determine the % inaccuracy by calculating the percent error of the micropipette at the set volume of 100 µL A. Standard deviation B. Covieffecrnt of varaiant C. % error (precision) Percent error = mean volume delivered -expected volume x 100 Expected volume RUN Weight Measurement (in g) 1 0.0985 2 0.0987 3 0.0985 4 0.0982 5 0.0984 6 0.0984 7 0.0981 8 0.0983 9 0.0982 10 0.0988 Total 0.9841 A. Standard deviation B. Covieffecrnt of varaiant C. % error (precision)Which is one of the following statements about WRONG about serum creatinine? Please select one: O A. It is used to estimate glomerular filtration rate b. Creatinine is not bound to protein in plasma c. Creatinine is only eliminated by kidney d. Creatinine urinary excretion rate is not affected by diseases e. Creatinine is constantly formed by muscle. Lineweaver-Burk plot is the most used linearization method of the MichaelisMenten equation, but the main drawback is a/an:a. overemphasis to low substrate concentration and less emphasis to high substrate concentration.b. overemphasis to high substrate concentration and less emphasis to low substrate concentration.c. exaggeration to both ends of the reciprocal of the substrate concentration.d. lack of independent variables to x- and y- coordinates.Kinetic data were gathered for Enzyme X, its substrate, and a known competitive inhibitor Z. Upon plotting the linearized kinetic data, one could surmise that the plot of the inhibited enzyme would have:a. a slope and y-intercept both lower in magnitude than the plot of the uninhibited enzyme using Eadie-Hofstee method.b. a constant slope and y-intercept that is lower in magnitude with the plot of the uninhibited enzyme using Eadie-Hofstee method.c. a slope and y-intercept greater in magnitude than the plot of the uninhibited enzyme using…
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