![Table 13: Rate of reaction in the presence and absence of inhibitors. V (mmolL/min 1 mM [S] mmol/lL 1 mM 3 mM 5 mM 0 Inhibitor 1.72 2.04 2.63 3.33 4.17 Inhibitor AInhibitor B Inhibitor BInhibitor B 1.25 1.67 2.5 0.98 1.17 1.47 1.96 2.38 1.52 1.85 2.30 3.14 3.91 1.25 1.54 2.01 2.86 3.72 1.01 1.26 1.72 2.56 3.49 10](http://img.homeworklib.com/questions/86efd9b0-b01f-11eb-877f-c9cc47634b94.png?x-oss-process=image/resize,w_560)
Use the values from Table 13 to generate a Table showing 1/[S] and 1/V Plot Lineweaver Burke (1/v vs. 1/[s]) and caculate Km and Vmax in the absence and presence of 1mM inhibitor A. What is the nature of inhibitor A?
Plot 1/V vs 1/[S], and caculate the values of Km and Vmax in the
absence and presence of 3 mM and 5mM of inhibitor B. What is the
nature of inhibitor B?
Plot 1/V vs [I] i .e Dixon plot using the data from inhibitor B
Please I really need help!
All the data is given
Homework Answers
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Use the values from Table 13 to generate a Table showing 1/[S]
and 1/V Plot Lineweaver...
please graph all 3 lines and explain the vmax&km How to: Lineweaver Burke 1. The following...
please graph all 3 lines and explain the
vmax&km
How to: Lineweaver Burke 1. The following data was determined for an enzyme in the absence of an inhibitor and in the presence of two different inhibitors (V2 and V3). Determine the V. and K for the enzyme (1) Plot the data and determine the type of inhibition for each inhibitor (S) mm 1 V2 4.3 5.5 V1 12 20 29 2 relliate 150b
The equation that describes the above Michaelis-Menten curve: Vo TS]+K Vmax [S] Michaelis-Menten Equation Lineweaver and...
The equation that describes the above Michaelis-Menten curve: Vo TS]+K Vmax [S] Michaelis-Menten Equation Lineweaver and Burke manipulated the Michaelis-Menten equation to yield: Ko V I S Vmax [S] Lineweaver-Burke Equation Linewenver Burke Equation If you plot 1/ V. vs. 1/[S], you get the following Lineweaver-Burke plot: 1/V. Slope = km/Vmax Intercept = -1/KM -Intercept = 1/Vmax 1/[S] Which is easier to calculate values for Km and Vmax, using the linear (y=mx+b) Lineweaver-Burke Plot or the Michaelis-Menten curve?
Please do everything like you were answering a test. Don’t attempt if youre not going to do all p...
Please do everything like you were answering a test. Don’t attempt
if youre not going to do all parts. Do it ASAP and I will give you
a good rating. If not I will report you. Thank you so much for
being the best. Show work if necessary and be concise. There’s no
way for me to separate so do all parts.
do all parts please. I cant seperate it because it will be
refunded.
2. i) (10 points) The...
Michaelis-Menten plot and Lineweaver-Burk plot calculations: Use provided data to generate both M-M and L-B plots....
Michaelis-Menten plot and Lineweaver-Burk plot calculations: Use provided data to generate both M-M and L-B plots. Use scatter plots with markers on Excel: On the M-M Plot: estimate Vmax, KM On the L-B Plot: determine Vmax, KM, keat, kcat/Km. The total enzyme concentration is 5 uM. Graphs can be 1/2 page. Must be computer generated with all axes labeled. Substrate (mM) V. (mM/s) | 1/[S] (mM1) 1/V. (s/mM) 10 | 0 2.73 5.45 8.17 10.9 40.4 0.124 0.181 0.212 0.228...
need B C and D done please please please help!!! 1. You measure the initial rate...
need B C and D done please please please help!!!
1. You measure the initial rate of an enzyme reaction as a function of substrate concentration in the presence and absence of an inhibitor. The following data was obtained: V. (-) Inhibitor (mm/min) (+) Inhibitor (mM/min) 17 [S] (MM) 0.0001 0.0002 0.0005 0.001 0.002 Please submit calculations and graph for full credit! Note: You are required to use Excel to generate the Lineweaver-Burk plot (a) (10 points) Create a Lineweaver-Burk...
5) (14 marks) The following kinetic data were obtained for an enzyme in the absence of...
5) (14 marks) The following kinetic data were obtained for an enzyme in the absence of inhibitor (1), and in the presence of an inhibitor at 5 mM concentration (2). Assume[ET] is the same in each experiment. [S] (MM) (1) v(umol/mL sec) 12 (2) v(umol/mL sec) 4.3 1 8 2 4 20 29 14 21 8 35 12 40 26 a. Using a graphing program (excel or sigmaplot) construct a lineweaver burke plot representing the uninhibited reaction and the inhibited...
i need help with part two PART TWO 1) The steady-state kinetics of an enzyme is studied in the absence and presence...
i
need help with part two
PART TWO 1) The steady-state kinetics of an enzyme is studied in the absence and presence of inhibitor A. The initial rate is given as a function of substrate concentration in the following table. [S] (MM) * Velocity in substrate only y (mM/min) .25 1.72 58 ,598 r.60 2.04 .44 50 A 2.63 238 5.00 .2 3.33 10.00 4.17 4 Velocity in substrate + S inhibitor A (MM/min) 0.98 1.02 | 1.17 . 5...
3. Below is a Lineweaver-Burke plot of an enzyme reaction in the presence and absence of...
3. Below is a Lineweaver-Burke plot of an enzyme reaction in the presence and absence of an inhibitor. 2.4 2.3 2.2 2.1 2 1.9 1.8 1.7 1.6 1.5 1.4 1.3 1.2 1.1 1 0.9 0.8 < 0.7 0.6 0.5 0.4 0.3 0.2 0.1 0 -0.1 -0.2 -0.3 -0.4 -0.5 -0.6 -0.7 -0.8 . . . . . -1 -0.9 -0.8 -0.7 -0.6 -0.5 -0.4 -0.3 -0.2 -0.1 O 0.1 0.2 0.3 0.4 0.5 0.6 0.7 0.8 0.9 1 1.1 1/[S]...
Prostaglandins are a class of eicosanoids (fatty acid derivatives) with a variety of extremely potent actions...
Prostaglandins are a class of eicosanoids (fatty acid derivatives) with a variety of extremely potent actions on vertebrate tissues. They are responsible for producing fever and inflammation and its associated pain. Prostaglandins are derived from the 20-carbon fatty acid, arachidonic acid, in a reaction catalyzed by the enzyme, prostaglandin endoperoxide synthase. This uses oxygen to convert arachidonic acid to PGG2 (a prostaglandin). Ibuprofen inhibits this enzyme and is a fever reducer and anti-inflammatory agent. The kinetic data is given below...
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)....
please graph all 3 lines and explain the
vmax&km
How to: Lineweaver Burke 1. The following data was determined for an enzyme in the absence of an inhibitor and in the presence of two different inhibitors (V2 and V3). Determine the V. and K for the enzyme (1) Plot the data and determine the type of inhibition for each inhibitor (S) mm 1 V2 4.3 5.5 V1 12 20 29 2 relliate 150b
The equation that describes the above Michaelis-Menten curve: Vo TS]+K Vmax [S] Michaelis-Menten Equation Lineweaver and Burke manipulated the Michaelis-Menten equation to yield: Ko V I S Vmax [S] Lineweaver-Burke Equation Linewenver Burke Equation If you plot 1/ V. vs. 1/[S], you get the following Lineweaver-Burke plot: 1/V. Slope = km/Vmax Intercept = -1/KM -Intercept = 1/Vmax 1/[S] Which is easier to calculate values for Km and Vmax, using the linear (y=mx+b) Lineweaver-Burke Plot or the Michaelis-Menten curve?
Please do everything like you were answering a test. Don’t attempt
if youre not going to do all parts. Do it ASAP and I will give you
a good rating. If not I will report you. Thank you so much for
being the best. Show work if necessary and be concise. There’s no
way for me to separate so do all parts.
do all parts please. I cant seperate it because it will be
refunded.
2. i) (10 points) The...
Michaelis-Menten plot and Lineweaver-Burk plot calculations: Use provided data to generate both M-M and L-B plots. Use scatter plots with markers on Excel: On the M-M Plot: estimate Vmax, KM On the L-B Plot: determine Vmax, KM, keat, kcat/Km. The total enzyme concentration is 5 uM. Graphs can be 1/2 page. Must be computer generated with all axes labeled. Substrate (mM) V. (mM/s) | 1/[S] (mM1) 1/V. (s/mM) 10 | 0 2.73 5.45 8.17 10.9 40.4 0.124 0.181 0.212 0.228...
need B C and D done please please please help!!!
1. You measure the initial rate of an enzyme reaction as a function of substrate concentration in the presence and absence of an inhibitor. The following data was obtained: V. (-) Inhibitor (mm/min) (+) Inhibitor (mM/min) 17 [S] (MM) 0.0001 0.0002 0.0005 0.001 0.002 Please submit calculations and graph for full credit! Note: You are required to use Excel to generate the Lineweaver-Burk plot (a) (10 points) Create a Lineweaver-Burk...
5) (14 marks) The following kinetic data were obtained for an enzyme in the absence of inhibitor (1), and in the presence of an inhibitor at 5 mM concentration (2). Assume[ET] is the same in each experiment. [S] (MM) (1) v(umol/mL sec) 12 (2) v(umol/mL sec) 4.3 1 8 2 4 20 29 14 21 8 35 12 40 26 a. Using a graphing program (excel or sigmaplot) construct a lineweaver burke plot representing the uninhibited reaction and the inhibited...
i
need help with part two
PART TWO 1) The steady-state kinetics of an enzyme is studied in the absence and presence of inhibitor A. The initial rate is given as a function of substrate concentration in the following table. [S] (MM) * Velocity in substrate only y (mM/min) .25 1.72 58 ,598 r.60 2.04 .44 50 A 2.63 238 5.00 .2 3.33 10.00 4.17 4 Velocity in substrate + S inhibitor A (MM/min) 0.98 1.02 | 1.17 . 5...
3. Below is a Lineweaver-Burke plot of an enzyme reaction in the presence and absence of an inhibitor. 2.4 2.3 2.2 2.1 2 1.9 1.8 1.7 1.6 1.5 1.4 1.3 1.2 1.1 1 0.9 0.8 < 0.7 0.6 0.5 0.4 0.3 0.2 0.1 0 -0.1 -0.2 -0.3 -0.4 -0.5 -0.6 -0.7 -0.8 . . . . . -1 -0.9 -0.8 -0.7 -0.6 -0.5 -0.4 -0.3 -0.2 -0.1 O 0.1 0.2 0.3 0.4 0.5 0.6 0.7 0.8 0.9 1 1.1 1/[S]...
Prostaglandins are a class of eicosanoids (fatty acid derivatives) with a variety of extremely potent actions on vertebrate tissues. They are responsible for producing fever and inflammation and its associated pain. Prostaglandins are derived from the 20-carbon fatty acid, arachidonic acid, in a reaction catalyzed by the enzyme, prostaglandin endoperoxide synthase. This uses oxygen to convert arachidonic acid to PGG2 (a prostaglandin). Ibuprofen inhibits this enzyme and is a fever reducer and anti-inflammatory agent. The kinetic data is given below...
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)....
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