You performed a kinetic study of the enzyme lipase and you obtained the following double reciprocal (Lineweaver-Burk) plot: 4 3 y = 4.3511x + 1.8889 -0.5 -0.3 -0.1 0.1 0.3 0.5 0.7 0.9 1/[S] When you performed the same kinetic study in the presence of an inhibitor, you obtained a new line that had y-intercept 3 and x-intercept -0.3. Based on this information select all correct statements about this inhibitor. This is mixed inhibitor. When this inhibitor is present apparent Km of enzyme decreases. This inhibitor prevents substrate from binding to the enzyme. This is uncompetitive inhibitor. When this inhibitor is present apparent Vmax of enzyme decreases. When this inhibitor is present apparent Km of enzyme increases. This inhibitor can bind to either enzyme or enzyme-substrate complex. OA/T

You performed a kinetic study of the enzyme lipase and you obtained the following double reciprocal (Lineweaver-Burk) plot: 4 3 y = 4.3511x + 1.8889 -0.5 -0.3 -0.1 0.1 0.3 0.5 0.7 0.9 1/[S] When you performed the same kinetic study in the presence of an inhibitor, you obtained a new line that had y-intercept 3 and x-intercept -0.3. Based on this information select all correct statements about this inhibitor. This is mixed inhibitor. When this inhibitor is present apparent Km of enzyme decreases. This inhibitor prevents substrate from binding to the enzyme. This is uncompetitive inhibitor. When this inhibitor is present apparent Vmax of enzyme decreases. When this inhibitor is present apparent Km of enzyme increases. This inhibitor can bind to either enzyme or enzyme-substrate complex. OA/T

Chemistry

10th Edition

ISBN:9781305957404

Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Chapter1: Chemical Foundations

Section: Chapter Questions

Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...

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0.9 The enzyme from the previous problem was further purified from the supernatant, after which a (Bradford) protein assay using coomassie blue was performed. The following standard curve was established using known concentrations of the enzyme. 595 0.8 0.7 0.6 0.5 80.4 0.3 0.2 0.1 y=0.5617x+0.0119 R²=0.9878 0 0.5 Protein Concentration (mg/mL) A. At what wavelength is the sample measured at? 1.5 B. Write out the equation relating OD595 and protein concentration. C. After purification, the protein sample was diluted 10-fold and then reacted with Coomassie Blue that resulted in an OD595 of 0.7. What was the concentration of protein in the supernatant? D. The purified protein was concentrated to a final volume of 1 L. What was the final amount of purified protein recovered? 200 g of the hulls initially at 25°C was placed into a perfectly insulated calorimeter with 500 g of isopropyl alcohol (IPA) at 5°C without stirring. At equilibrium, the temperature of the IPA was found to be 13.7°C. =…