You perform a series of enzyme activity assays and then graph the data using a Lineweaver-Burk...
You perform a series of enzyme activity assays and then graph the data using a Lineweaver-Burk plot. You determine the X-intercept is at -0.02 mM-1 and the Y-intercept is at 5.0 (mM/sec)-1. Calculate the Vmax and Km for this enzyme.
A. Vmax = 0.20 mM/sec; Km = 50.0 mM
B. Vmax = 0.20 mM/sec; Km = ‒50.0 mM
C. Vmax = 5.0 mM/sec; Km = 0.02 mM
D. Vmax = 5.0 mM/sec; Km = ‒0.02 mM
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You perform a series of enzyme activity assays and then graph the data using a Lineweaver-Burk...
4. The following data were obtained from an enzyme kinetics experiment. Graph the data using a...
4. The following data were obtained from an enzyme kinetics experiment. Graph the data using a Lineweaver-Burk plot and determine, by inspection of the graph, the values for Km and Vmax. ISI (M) V (nmol/min) 0.20 0.26 0.33 1.00 1.43 1.67 2.08 3.33 5. You measured the kinetics of an enzyme activity as a function of substrate concentration (see Table). The enzyme concentration was maintained constant at a level of 1 M. [S] AM Vopmol/min 2.9 3.8 4.4 Plot the...
LINEWEAVER-BURK plot 1. You perform the hydrolysis reaction as required in the lab experiment, and the...
LINEWEAVER-BURK plot 1. You perform the hydrolysis reaction as required in the lab experiment, and the final reading on your blood glucose meter for one of your samples is 385 mg/dL. You need your data to be in units of mm (millimolar, which is millimoles per liter, abbreviated as mmol/L). Show, in a step-by-step conversion, how you would convert 385 mg/dL to the proper answer in mM. 385 mg dlº= ?mm immoles 2. Assuming that the reaction occurred over a...
After collecting enzyme kinetics data using substrates in mM and reaction velocities in mM/min, you make...
After collecting enzyme kinetics data using substrates in mM and reaction velocities in mM/min, you make a Lineweaver-Burk plot. Your line of best fit has the equation: y = 0.00160 x + 0.00759. Calculate the Vmax of the enzyme using the equation: 1 KM 1 - = v Vmax [S] Vmax +
9. The following data were obtained from an enzyme kinetics experiment. Graph the data using a...
9. The following data were obtained from an enzyme kinetics experiment. Graph the data using a Lineweaver-Burk plot and determine the values for Km and Vmax. [S] (UM) V(nmol/min) 0.20 0.26 1.43 1.67 2.08 3.33 0.33 1.00
how do you make a lineweaver-burk plot where the trend line extends backwards? is there a...
how do you make a lineweaver-burk plot where the trend line
extends backwards? is there a way of figuring out how far back it
should extend based of your data ? As well, how do you plot two
sets of data on one graph ? Thank you! (idk if you need to see my
data-> attached below)
Biochemistry Enzyme Kinetics Assignment Four answers for this assignment will be completed in elearn: En in elearn: Enzyme Kinetics Quiz ots but must...
The Lineweaver-Burke Plot for the enzyme in question 1 is shown below. In this plot, the...
The Lineweaver-Burke Plot for the enzyme in question 1 is shown below. In this plot, the y intercept (0.019153) is 1/vmax and the x intercept (-0.0449) is -1/km. What are the exact km and vmax based on this graph (show your work)? Km= Vmax=
Q2) Using the data in the below table, which were obtained for enzyme activity without presence...
Q2) Using the data in the below table, which were obtained for enzyme activity without presence of inhibitors. [15 points) IS (MM) 1.3 2.6 6.5 13.0 26.0 VomM/s) 2.50 4.00 6.30 7.60 9.00 A) Draw Lineweaver-Burk plot and determine the K. and Vmax for this uninhibited enzyme. (You may use hand, excel or other program to draw the graph and find the equation. Then copy and paste the graph here, you need to show axis labels) [6 points) B) From...
16. At right is a graph obtained from a series of enzyme kinetics assays. The Vmax...
16. At right is a graph obtained from a series of enzyme kinetics assays. The Vmax for this enzyme and substrate is 4.5 uM/s. 5 4.5 4 a) What is the KM? KM: v. (mM/s) 3.5 3 2.5 2 1.5 1 0.5 b) If a pure non-competitive inhibitor was added to the assays, what would the resulting kinetics curve be like? Give a Km and Vmax in the presence of the inhibitor (write them below) and draw an appropriate curve...
CHEM3250 Assignment-Enzyme Inhibition Consider the data below for an enzyme catalyzed reaction. T...
CHEM3250 Assignment-Enzyme Inhibition Consider the data below for an enzyme catalyzed reaction. The rate of the reaction has been determined with and without an inhibitor. A total concentration of enzyme of 20 uM was used in the experiment. SHOW WORK AND UNITS!!! Without Inhibitor With Inhibitor [substrate] (mM)Rate of formation of te of formation of product product (mM/min) mM/min) 6.67 5.25 0.49 7.04 38.91 1.0 2.2 6.9 41.8 44.0 1.5 3.5 1 a) On the same graph, plot the data...
4. The double-reciprocal transformation of the Michaelis-Menten equation, also called the Lineweaver-Burk plot, is give...
4. The double-reciprocal transformation of the Michaelis-Menten equation, also called the Lineweaver-Burk plot, is given by: 1 Km 1 1 where, the plot of (1/V.) vs (1/[S]) is a linear plot. If you only know the x-axis and y-axis intercepts from this plot, how can you determine Vmax and Km? (A) multiply the reciprocal of the x-axis intercept by -1. (B) multiply the reciprocal of the y-axis intercept by -1. (C) take the reciprocal of the x-axis intercept. (D) take...
4. The following data were obtained from an enzyme kinetics experiment. Graph the data using a Lineweaver-Burk plot and determine, by inspection of the graph, the values for Km and Vmax. ISI (M) V (nmol/min) 0.20 0.26 0.33 1.00 1.43 1.67 2.08 3.33 5. You measured the kinetics of an enzyme activity as a function of substrate concentration (see Table). The enzyme concentration was maintained constant at a level of 1 M. [S] AM Vopmol/min 2.9 3.8 4.4 Plot the...
LINEWEAVER-BURK plot 1. You perform the hydrolysis reaction as required in the lab experiment, and the final reading on your blood glucose meter for one of your samples is 385 mg/dL. You need your data to be in units of mm (millimolar, which is millimoles per liter, abbreviated as mmol/L). Show, in a step-by-step conversion, how you would convert 385 mg/dL to the proper answer in mM. 385 mg dlº= ?mm immoles 2. Assuming that the reaction occurred over a...
After collecting enzyme kinetics data using substrates in mM and reaction velocities in mM/min, you make a Lineweaver-Burk plot. Your line of best fit has the equation: y = 0.00160 x + 0.00759. Calculate the Vmax of the enzyme using the equation: 1 KM 1 - = v Vmax [S] Vmax +
9. The following data were obtained from an enzyme kinetics experiment. Graph the data using a Lineweaver-Burk plot and determine the values for Km and Vmax. [S] (UM) V(nmol/min) 0.20 0.26 1.43 1.67 2.08 3.33 0.33 1.00
how do you make a lineweaver-burk plot where the trend line
extends backwards? is there a way of figuring out how far back it
should extend based of your data ? As well, how do you plot two
sets of data on one graph ? Thank you! (idk if you need to see my
data-> attached below)
Biochemistry Enzyme Kinetics Assignment Four answers for this assignment will be completed in elearn: En in elearn: Enzyme Kinetics Quiz ots but must...
Q2) Using the data in the below table, which were obtained for enzyme activity without presence of inhibitors. [15 points) IS (MM) 1.3 2.6 6.5 13.0 26.0 VomM/s) 2.50 4.00 6.30 7.60 9.00 A) Draw Lineweaver-Burk plot and determine the K. and Vmax for this uninhibited enzyme. (You may use hand, excel or other program to draw the graph and find the equation. Then copy and paste the graph here, you need to show axis labels) [6 points) B) From...
16. At right is a graph obtained from a series of enzyme kinetics assays. The Vmax for this enzyme and substrate is 4.5 uM/s. 5 4.5 4 a) What is the KM? KM: v. (mM/s) 3.5 3 2.5 2 1.5 1 0.5 b) If a pure non-competitive inhibitor was added to the assays, what would the resulting kinetics curve be like? Give a Km and Vmax in the presence of the inhibitor (write them below) and draw an appropriate curve...
CHEM3250 Assignment-Enzyme Inhibition Consider the data below for an enzyme catalyzed reaction. The rate of the reaction has been determined with and without an inhibitor. A total concentration of enzyme of 20 uM was used in the experiment. SHOW WORK AND UNITS!!! Without Inhibitor With Inhibitor [substrate] (mM)Rate of formation of te of formation of product product (mM/min) mM/min) 6.67 5.25 0.49 7.04 38.91 1.0 2.2 6.9 41.8 44.0 1.5 3.5 1 a) On the same graph, plot the data...
4. The double-reciprocal transformation of the Michaelis-Menten equation, also called the Lineweaver-Burk plot, is given by: 1 Km 1 1 where, the plot of (1/V.) vs (1/[S]) is a linear plot. If you only know the x-axis and y-axis intercepts from this plot, how can you determine Vmax and Km? (A) multiply the reciprocal of the x-axis intercept by -1. (B) multiply the reciprocal of the y-axis intercept by -1. (C) take the reciprocal of the x-axis intercept. (D) take...
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