Question

LINEWEAVER-BURK plot 1. You perform the hydrolysis reaction as required in the lab experiment, and the final reading on your
3. You use a bone alkaline phosphatase enzyme to cleave the phosphate group from phenyl phosphate at various concentrations o
0 0
Add a comment Improve this question Transcribed image text
Answer #1

Reading in blood glucose meter is 385 mg/dL

= 385 × ( 10-3 g/10-1 L)

= 3.85 g/L

Now molecular weight of glucose=180

So no of moles of glucose per litre = (3.85/180)

=0.0214

So concentration of glucose = 0.0214 M

= 0.0214 × 103 mM

= 21.4 mM

2. As the reaction has occured over 30 minutes so rate of reaction

= Change in concentration/ time

= (21.4/30)mM/min

=0.7133 mM/min.

Add a comment
Know the answer?
Add Answer to:
LINEWEAVER-BURK plot 1. You perform the hydrolysis reaction as required in the lab experiment, and the...
Your Answer:

Post as a guest

Your Name:

What's your source?

Earn Coins

Coins can be redeemed for fabulous gifts.

Not the answer you're looking for? Ask your own homework help question. Our experts will answer your question WITHIN MINUTES for Free.
Similar Homework Help Questions
  • 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

  • Please help me with these two problems. I will rate the answers. 1. The HIV-1 protease,...

    Please help me with these two problems. I will rate the answers. 1. The HIV-1 protease, an important enzyme in the life cycle of the human immunodeficiency virus-1 (HIV-1), is a good drug target for the treatment of HIV and AIDS. A protein produced by the virus, p6*, is an HIV-1 protease inhibitor. The activity of the HIV-1 protease was measured in the presence and absence of p6* using an assay involving an artificial substrate, as shown below. NH Lys...

  • (I need help with part C, Drawing the expected Michaelis-Menten plot; Do NOT draw the Lineweaver-Burk...

    (I need help with part C, Drawing the expected Michaelis-Menten plot; Do NOT draw the Lineweaver-Burk plot. thanks!) 1. Michaelis-Menten kinetics- use the M-M equation to answer the following: a. An enzyme (5 µM) has a Vmax of 450 mM/min. What is kcat? b. When the substrate concentration is 50 mM, the initial velocity (V0) was measured to be 375 mM/min. Under the conditions described above, calculate the KM. c. Draw the expected Michaelis-Menten plot (label your axes and include...

  • 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...

  • 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 +

  • 11. In Excel, prepare Lineweaver-Burk plots for the behavior of an enzyme for which the following...

    11. In Excel, prepare Lineweaver-Burk plots for the behavior of an enzyme for which the following experimental data are available: V, umol/min umol/min (No Inhibitor) S], mM (Inhibitor Present) 3.66 5.12 6.18 6.98 7.60 4.58 6.40 7.72 8.72 9.50 3.0 5.0 7.0 9.0 11.0 a. What are the KM and Vmax values for the inhibited and uninhibited reaction 5 pts. each reaction) b. Is the inhibitor competitive or noncompetitive? (5 pts.) Micheli-Menten) EQUATIONS: VV

  • 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...

  • ] a. The equation of Lineweaver-Burk double-reciprocal plot of caffeine dehydrogenase-catalyzed reaction is   y = 12x...

    ] a. The equation of Lineweaver-Burk double-reciprocal plot of caffeine dehydrogenase-catalyzed reaction is   y = 12x + 3. Calculate Vmax (mmol/s) and Km (mmol/L). b. [5 points] Estimate V for caffeine concentration of 400 mmol/L. c. [10 points] The enzyme caffeine dehydrogenase (Cdh) is an inducible quinone-dependent oxidoreductase. Describe how the addition of caffeine into the culture medium will be detected and transcriptionally regulated by the two-component system in Pseudomonas sp. CBB1.

  • Can help me with these questions please. 30. Sphingosine-1-phosphate (S1P) is important for cell survival. The...

    Can help me with these questions please. 30. Sphingosine-1-phosphate (S1P) is important for cell survival. The synthesis of S1P from sphingosine and ATP is catalyzed by the enzyme sphingosine kinase. The velocity of the sphingosine kinase reaction was measured in the presence and absence of threo-sphingosine, a stereoisomer of sphingosine that inhibits the enzyme. The results are shown below. Sphingosine (uM) vo (mg /min) vo (mg /min) with inhibitor 2.5 32.3 8.5 3.5 40 11.5 5.0 50.8 14.6 10 72...

  • 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...

ADVERTISEMENT
Free Homework Help App
Download From Google Play
Scan Your Homework
to Get Instant Free Answers
Need Online Homework Help?
Ask a Question
Get Answers For Free
Most questions answered within 3 hours.
ADVERTISEMENT
ADVERTISEMENT
ADVERTISEMENT