3) Enzyme kinetics are determined under initial rate conditions, wherein the initial substrate concentrations changes very...
3) Enzyme kinetics are determined under initial rate conditions, wherein the initial substrate concentrations changes very little, because:
(A) Products do not accumulate and inhibit the forward reaction
(B) Enzymes are unstable under most assay conditions, and rapidly lose activity
(C) The substrate concentration does not change appreciably and so does not create an additional variable
(D) All of the above
(E) Some of the above
Homework Answers
Enzyme kinetics are determined under initial rate conditions, wherein the initial substrate concentrations changes very little, because
(A) Products do not accumulate and inhibit the forward reaction (correct option)
Add Answer to:
3) Enzyme kinetics are determined under initial rate conditions,
wherein the initial substrate concentrations changes very...
Enzyme Kinetics Problem The initial rate for an enzyme-catalyzed reaction has been determined at a number...
Enzyme Kinetics Problem The initial rate for an enzyme-catalyzed reaction has been determined at a number of substrate concentrations. Data are given below: 5 27 23 65 1. Estimate V and K from a Michaelis-Menten graph of V versus [S] 2. Use a Lineweaver-Burk plot to analyze the same data. a. Determine V and Ka from the Lineweaver-Burk BONUS: If the total enzyme concentration was I nmol/L, what is K?
Enzyme Kinetics Problem The initial rate for an enzyme-catalyzed reaction...
1. The kinetics of an enzyme was examined at various substrate concentrations in both the presence...
1. The kinetics of an enzyme was examined at various substrate concentrations in both the presence and absence of 3 mM inhibitor Z. The initial velocity data obtained are shown below: [S] (mmoles liter) v (mmoles"litermin) no inhibitor inhibitor Z 1.25 1.67 2.50 5.00 10.0 1.72 2.04 2.63 3.33 4.17 0.98 1.17 1.47 1.96 2.38 (4 pts) Estimat e Vmax and Kw in the presence and absence of inhibitor using the Michaelis Menton curve-fitting program on Kaleidagraph (see lab manual)....
Under what circumstances does an enzyme catalyzed reaction rate resemble a non-enzyme catalyzed reaction? At very...
Under what circumstances does an enzyme catalyzed reaction rate resemble a non-enzyme catalyzed reaction? At very low concentrations of substrate (Km is greater than S) the Michaelis-Menton equation can be simplified to? At very high concentrations of substrate, the Michaelis-Menton equation can be simplified to? How do you determine the initial rate of reaction
Enzyme Kinetics Lab Guide Table 2: Absorbance values per minute for varied substrate concentrations Time (min)...
Enzyme Kinetics Lab Guide Table 2: Absorbance values per minute for varied substrate concentrations Time (min) Tube A (0mM) Tube B (2.0mM) Tube C (5.0mM) Tube D (8.0mM) Tube E (12.0mM) Tube F (20.0mM) 0 0 0.012 0.066 0.066 0.076 0.191 1 0.011 0.045 0.128 0.128 0.164 0.200 2 0.017 0.096 0.190 0.190 0.219 0.241 3 0.009 0.122 0.234 0.234 0.294 0.313 Table 3. Absorbance values versus substrate concentration at a constant time (from Table 2) Concentration (mM) 0 mM...
2. hypothesize the best conditions (pH and temperature) under which the enzyme chymotrypsin functions with an...
2. hypothesize the best conditions (pH and temperature) under
which the enzyme chymotrypsin functions with an appropriate
reference. also, hypothesize what will occur in the presence of an
inhibitor and the type of inhibition.
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Based on the document below, 1. Describe the hypothesis Chaudhuri et al ids attempting to evaluate;...
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
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CHAUDHURI et al: KINETIC BEHAVIOUR OF CALF INTESTINAL ALP WITH PNPP 8.5, 9, 9.5, 10,...
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Please read the article and answer about questions. You and the Law Business and law are...
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Enzyme Kinetics Problem The initial rate for an enzyme-catalyzed reaction has been determined at a number of substrate concentrations. Data are given below: 5 27 23 65 1. Estimate V and K from a Michaelis-Menten graph of V versus [S] 2. Use a Lineweaver-Burk plot to analyze the same data. a. Determine V and Ka from the Lineweaver-Burk BONUS: If the total enzyme concentration was I nmol/L, what is K?
Enzyme Kinetics Problem The initial rate for an enzyme-catalyzed reaction...
1. The kinetics of an enzyme was examined at various substrate concentrations in both the presence and absence of 3 mM inhibitor Z. The initial velocity data obtained are shown below: [S] (mmoles liter) v (mmoles"litermin) no inhibitor inhibitor Z 1.25 1.67 2.50 5.00 10.0 1.72 2.04 2.63 3.33 4.17 0.98 1.17 1.47 1.96 2.38 (4 pts) Estimat e Vmax and Kw in the presence and absence of inhibitor using the Michaelis Menton curve-fitting program on Kaleidagraph (see lab manual)....
2. hypothesize the best conditions (pH and temperature) under
which the enzyme chymotrypsin functions with an appropriate
reference. also, hypothesize what will occur in the presence of an
inhibitor and the type of inhibition.
EXPERIMENT 5: ENZYME ACTIVITY WITH a-CHYMOTRYPSIN Prelab Assignment 1. Prepare a flow chart, covering one half of the experimental work (either part A and C if your lab bench is on the window side of the lab or part B and D if your locker is...
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,...
1. According to the paper, what does lactate dehydrogenase
(LDH) do and what does it allow to happen within the myofiber? (5
points)
2. According to the paper, what is the major disadvantage of
relying on glycolysis during high-intensity exercise? (5
points)
3. Using Figure 1 in the paper, briefly describe the different
sources of ATP production at 50% versus 90% AND explain whether you
believe this depiction of ATP production applies to a Type IIX
myofiber in a human....
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