Given the following data (generated from a series of assays), what is the Km and Vmax for this enzyme? Include units and be careful of significant figures.
[S], μM | V(μM/min) |
10.0 | 32.4 |
25.0 | 66.3 |
50.0 | 102 |
150.0 | 160 |
300.0 | 185 |
Here, V max is 185micro,M/min and Km is that value of x axis which corresponds to the value of Vmax/2 in the y axis. Here, Km is 43.6microM.
Given the following data (generated from a series of assays), what is the Km and Vmax...
16. At right is a graph obtained from a series of enzyme kinetics assays. The Vmax for this enzyme and substrate is 4.5 uM/s. 5 4.5 4 a) What is the KM? KM: v. (mM/s) 3.5 3 2.5 2 1.5 1 0.5 b) If a pure non-competitive inhibitor was added to the assays, what would the resulting kinetics curve be like? Give a Km and Vmax in the presence of the inhibitor (write them below) and draw an appropriate curve...
16. At right is a graph obtained from a series of enzyme kinetics assays. The Vmax for this enzyme and substrate is 4.5 uM/s. a) What is the KM? 5 4.5 4 3.5 3 2.5 2 KM: 3mm V. (mM/s) 1.5 1 b) If a pure non-competitive inhibitor was added to the assays, what would the resulting kinetics curve be like? Give a Km and Vmax in the presence of the inhibitor (write them below) and draw an appropriate curve...
You perform a series of enzyme activity assays and then graph the data using a Lineweaver-Burk plot. You determine the X-intercept is at -0.02 mM-1 and the Y-intercept is at 5.0 (mM/sec)-1. Calculate the Vmax and Km for this enzyme. A. Vmax = 0.20 mM/sec; Km = 50.0 mM B. Vmax = 0.20 mM/sec; Km = ‒50.0 mM C. Vmax = 5.0 mM/sec; Km = 0.02 mM D. Vmax = 5.0 mM/sec; Km = ‒0.02 mM
The following observations come from Lineweaver-Burke plots, based on kinetic data generated from a Michaelis/Menton-type enzyme (E) that catalyzes the hydrolysis of a peptide substrate (S). All data were generated in the presence of 18.0 μM total enzyme. The enzyme-catalyzed reaction has a Km of 3.00 μM and a Vmax of 2.00 μM/sec. The enzyme-catalyzed reaction in the presence of 15.0 μM of Inhibitor A has an apparent Km of 2.25 μM and an apparent Vmax of 1.50 μM/sec. The...
Interpret the data above 1. What is the aporoximate Km and Vmax (units matter) 2.Briefly explain how you found each 3.if you used 0.020 microM enzyme in your studies, what is kcat in units of s^-1? Show your work units matter 4. Does this enzyme appear to display cooperativity? Explain how you came up to that conclusion. Directions: Below are data from 4 separate experiments that you must analyze/evaluate. Using the information from all 4 experiments, you must then propose...
The value of Km for the shown data for a hexokinase-catalyzed reaction is with the unit of . The value of Vmax for. the same reaction is with the unit of . Be sure to give the values with the correct number of significant figures. You might have to construct a kinetic plot. For units, choose one answer from (uM, 1/ UM, HM/second, uM x second, mM, 1/mM, second, 1/second, mM/second, mM x second) vo (mM/sec) Glucose concentration (mm) 0.10...
Based on the document below, 1. Describe the hypothesis Chaudhuri et al ids attempting to evaluate; in other words, what is the goal of this paper? Why is he writing it? 2. Does the data presented in the paper support the hypothesis stated in the introduction? Explain. 3.According to Chaudhuri, what is the potential role of thew alkaline phosphatase in the cleanup of industrial waste. CHAUDHURI et al: KINETIC BEHAVIOUR OF CALF INTESTINAL ALP WITH PNPP 8.5, 9, 9.5, 10,...
CASE 1-5 Financial Statement Ratio Computation Refer to Campbell Soup Company's financial Campbell Soup statements in Appendix A. Required: Compute the following ratios for Year 11. Liquidity ratios: Asset utilization ratios:* a. Current ratio n. Cash turnover b. Acid-test ratio 0. Accounts receivable turnover c. Days to sell inventory p. Inventory turnover d. Collection period 4. Working capital turnover Capital structure and solvency ratios: 1. Fixed assets turnover e. Total debt to total equity s. Total assets turnover f. Long-term...