what is the purpose of staggering the start and stop of the reactions? With reference to your experimental protocol, what is the purpose of staggering the start and stop of the reactions? A.To ensure that the reaction occurs with different amounts of enzyme in each tube so as to ensure comparability between reaction tubes. B.To ensure that the reaction occurs at exactly the same pH in each tube so as to ensure comparability between reaction tubes. C.To ensure that the reaction occurs for exactly the same time interval (30 minutes) in each tube so as to ensure comparability between reaction tubes. D.To ensure that the reaction occurs with exactly the same amount of substrate in each tube so as to ensure comparability between reaction tubes.

what is the purpose of staggering the start and stop of the reactions? With reference to your experimental protocol, what is the purpose of staggering the start and stop of the reactions? A.To ensure that the reaction occurs with different amounts of enzyme in each tube so as to ensure comparability between reaction tubes. B.To ensure that the reaction occurs at exactly the same pH in each tube so as to ensure comparability between reaction tubes. C.To ensure that the reaction occurs for exactly the same time interval (30 minutes) in each tube so as to ensure comparability between reaction tubes. D.To ensure that the reaction occurs with exactly the same amount of substrate in each tube so as to ensure comparability between reaction tubes.

Principles Of Radiographic Imaging: An Art And A Science

6th Edition

ISBN:9781337711067

Author:Richard R. Carlton, Arlene M. Adler, Vesna Balac

Publisher:Richard R. Carlton, Arlene M. Adler, Vesna Balac

Chapter6: X-ray Equipment

Section: Chapter Questions

Problem 6RQ

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s) In two experiments carried out in a research lab, an enzyme reaction is run with and without an inhibitor. Samples were taken over time to measure the concentration of product as the reaction proceeds, with raw data given below. Data were collected at 34 °C and pH 7.5, using [S] = 0.115 M (for both trials) & [E], = 0.0024 M (for both trials): Product concentration (mol P/L) No inhibitor [1] = 0.019 M 0 0 0.0011 0.0023 0.0031 0.0045 0.0074 0.0119 0.0195 0.0271 0.0410 0.0479 0.0550 0.0588 0.0600 Time min 0 3.5 9 13 17 26 43 69 104 156 208 311 415 519 0.0016 0.0038 0.0052 0.0078 0.0111 0.0180 0.0281 0.0412 0.0525 0.0587 0.0598 0.0600 0.0600 A. Determine the initial reaction velocities for both reactions. B. From these data, can you determine what type of inhibition is occurring? If so, show evidence of the type of inhibition occurring. If not, describe what experiment(s) should be done to determine the type of inhibition (competitive, non-competitive or uncompetitive), as well as how…
You will perform the protocol below for the calf intestinal alkaline phosphatase (CIP) provided. For each reaction, your final enzyme concentration should be 10 nM CIP. Note: Enzymes purchased are typically labelled with their “units of activity” (U), as this relates to how much enzyme is needed to catalyze a reaction. The 100 nM CIP provided has approximately 3 U/mL and was diluted 1 in 1,000 from a 500 U/mL purchased enzyme. 1) Create a table (similar to the one below) to help you determine and keep track of what to add to each of the cuvettes in which your reactions will be measured. The five different concentrations of PNPP should be: 25, 50, 100, 200, 300 μM. Each reaction will be in a final volume of 1 mL and contain 10 nM alkaline phosphatase. Concentrations of stock solutions: 1.0 mM PNPP, 100 nM calf intestinal phosphatase
Lisa decides to obtain values for the Km and Vmax of an enzyme that was isolated from liver cells.. Using the Michaelis Menten plot. In what kind of measurements are needed and what would be needed to plot on a graph to estimate Km and Vmax?
During a test of kinetics of an enzyme-catalyzed reaction, the following data were recorded: a. Determine the Michaelis-Menten constant for the reaction with no inhibitor present at 30 °C and at 49.6 °C. b. Determine the maximum velocity of the uninhibited reaction at 30 °C and an enzyme concentration of 1.6 g/L. c. Determine the Ki for the inhibitor at 30 °C and decide what type of inhibitor is being used.
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An enzymes catalyzed reaction is studied in the presence and absence of an inhibitor. The following data was obtained in the image provided. Plot 1/[S] as abscissa and 1/V as ordinate for both catalyzed reactions and reaction with inhibitor. Use the same graph for both plots Calculate the following: Km of enzyme in the reaction without inhibitor Km' of the enzyme in the reation with inhibitor Vmax of the uninhibited reaction Vmax of the inhibited reaction What kind of inhibitor was added to the enzyme catalyzed reaction? Explain your answer in terms of changes in Km and Vmax.
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An enzymes catalyzed reaction is studied in the presence and absence of an inhibitor. The following data was obtained in the image provided. Plot 1/[S] as abscissa and 1/V as ordinate for both catalyzed reactions and reaction with inhibitor. Use the same graph for both plots Michaelis–Menten kinetics Lineweaver–Burk plot Calculate the following: Km of enzyme in the reaction without inhibitor Km' of the enzyme in the reation with inhibitor Vmax of the uninhibited reaction Vmax of the inhibited reaction What kind of inhibitor was added to the enzyme catalyzed reaction? Explain your answer in terms of changes in Km and Vmax.
You have obtained experimental kinetic data for two versions of the same enzyme, a wild‑type and a mutant differing from the wild‑type at a single amino acid. The data are given in the table. Compare the kinetic parameters of the two versions using the data in the table. Assuming a two-step reaction scheme in which ?−1 is much larger than ?2, which of the following statements are correct? The mutant version has a higher affinity for the substrate. The wild‑type version requires a greater concentration of substrate to achieve ?maxVmax. The wild‑type version has a higher affinity for the substrate. The mutant version requires a greater concentration of substrate to achieve ?maxVmax. Calculate the initial velocity of the reaction catalyzed by the wild‑type enzyme when the substrate concentration is 10 mM. The reaction equilibrium is reached once there is no net change in the concentration of the substrate or the product. Based on the data table and your initial…
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With reference to your experimental protocol, why does adding the reaction mix to the “stop” tubes immediately stop the enzymic reaction? A.Stop tubes contain acid molybdate and the high pH of this reagent will denature the alkaline phosphatase, which has an optimal pH of 9.0. B.Stop tubes contain acid molybdate and the high pH of this reagent will denature the alkaline phosphatase, which has an optimal pH of 6.0. C.Stop tubes contain acid molybdate and the low pH of this reagent will denature the alkaline phosphatase, which has an optimal pH of 9.0. D.Stop tubes contain acid molybdate and the low pH of this reagent will denature the alkaline phosphatase, which has an optimal pH of 6.0.