II. The graph on the right shows the Lineweaver-Burk plots derived from 1/V (umoles/min)1 4.5 kinetic data obtained for flu virus +Relenza enzyme activity as a function of substrate concentration in the presence 4 3.5 and absence of two antiviral inhibitor drugs +Tamiflu 2.5 2 No inhibitor 1.5 -15 -10 -5 0 5 10 15 1/S (HM)1 1. Based on the Lineweaver-Burk plots, determine the Km and Vmax for each condition. Do NOT forget the units. Answers can be expressed either as a fraction or in decimals. No inhibitor: Km Vmax Tamiflu: Km Vmax Relenza: Km = Vmax=

II. The graph on the right shows the Lineweaver-Burk plots derived from 1/V (umoles/min)1 4.5 kinetic data obtained for flu virus +Relenza enzyme activity as a function of substrate concentration in the presence 4 3.5 and absence of two antiviral inhibitor drugs +Tamiflu 2.5 2 No inhibitor 1.5 -15 -10 -5 0 5 10 15 1/S (HM)1 1. Based on the Lineweaver-Burk plots, determine the Km and Vmax for each condition. Do NOT forget the units. Answers can be expressed either as a fraction or in decimals. No inhibitor: Km Vmax Tamiflu: Km Vmax Relenza: Km = Vmax=

Principles of Instrumental Analysis

7th Edition

ISBN:9781305577213

Author:Douglas A. Skoog, F. James Holler, Stanley R. Crouch

Publisher:Douglas A. Skoog, F. James Holler, Stanley R. Crouch

Chapter34: Particle Size Determination

Section: Chapter Questions

Problem 34.10QAP

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Calculate the slope on a Lineweaver-Burk plot (Km / Vmax) for the lactase reaction with inhibitor X. (inhibitor X changes lactase activity to a Vo of 0.10 mM per minute when [S] = 1.0 mM, and a Vo of 0.133333333333 mM per minute when [S] = 2.0 mM) 0.20 per minute 0.50 per minute 1.0 per minute 2.0 per minute 5.0 per minute
If the enzyme lactase has a Vo of 0.111111111111 mM per minute when [S] = 1.0 mM, and a Vo of 0.20 mM per minute when [S] = 5.0 mM, what is its Km? Calculate Vmax of the above enzyme (lactase). Calculate the slope on a Lineweaver-Burk plot (Km/Kmax) for the above enzyme (lactase).
If inhibitor X changes lactase activity to a Vo of 0.10 mM per minute when [S] = 1.0 mM, and a Vo of 0.133333333333 mM per minute when [S] = 2.0 mM, calculate the new Vmax. Calculate the new Km of the above lactase reaction, with inhibitor X. Calculate the slope on a Lineweaver-Burk plot (Km / Vmax) for the lactase reaction with inhibitor X. Inhibitor X exerts which of the following effects on the above enzyme (lactase)?
Provided in the Table below kinetic data for an enzymatic reaction that was carried out in the presence (last two columns) and absence (second column = control) of enzyme inhibitor. Both inhibitors were added in eachreaction at a concentration of 2 mM. The enzyme concentration was similar in all and was approximately 0.001 µM. a. Calculate both Vmax and KM for the control using Lineweaver-Burk curve. b. Provide the type of inhibition for both? c. Find, KI, for the inhibitor binding to the enzyme, for experiments (2) and (3). d. Calculate the reaction Kcat for the Control in experiment (1). e. Draw a velocity versus [S] showing Michaelis-Menten curve for the Control. Clearly show Vmax and KM for the enzyme.
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18. Jet is an undergraduate chemistry student, he’s out in the laboratory trying to determine the volatile organic compounds as well as overall protein content of the leaf and stem of a malunggay (Moringa oleifera). He subjected the leaf and stem in a separate digestion reaction (treatment of sulfuric acid), afterwards he subjected the products to high temperature induction to get a dry ash like substance. Which type/s of chemical analysis did Jet employ to reach his objective?I. Qualitative AnalysisII. Quantitative Analysis III. Instrumental Chemical AnalysisIV. Wet Chemical AnalysisA. II & IV onlyB. I & IV onlyC. I, II & IV onlyD. I, II, III, IV
Give the Vmax and Km for this enzyme that obeys Michaelis-Menten kinetics. Use 2 sig figs.
Three large proteins are ionized at the pH at which an electrical FFF separation is carried out. (i) if the ions are designated A2+, B2+, and C3+, predict the order of elution. (ii) What is FFF? (iii) List the four subtechniques of FFF.
An enzyme-catalyzed reaction is studied in the absence and presence of an inhibitor and the following data was obtained. [S] in mmoles/L Velocity in mmoles/L/min-1 No inhibitor With inhibitor 1.25 1.72 0.98 1.67 2.04 1.17 2.50 2.63 1.47 5.00 3.33 1.96 10.00 4.17 2.38 Calculate the Km of the enzyme in the reaction without inhibitor ________________________ Km’ of the enzyme in the reaction with inhibitor ________________________ Vmax of the uninhibited reaction ________________________ Vmax’ of the inhibited reaction ________________________
Using the kinetic data pictured, estimate Vmax and Km for the catalysis of Substrate 1 by the following enzyme (using the correct units).