In your acid phosphatase enzyme kinetics lab, you constructed a Lineweaver-Burk plot. Lefs assume that yougraphicaly obtain 1/Vmax - 9.33 (umoliey and -1Km--0.012 M. Which of the following is correct?A) Vmax = 9.33 (no units)B) Km = 0.012 (no units)C) Vmax = (1/Vru" = 0.107 umolisD) Km =-14-1K = 83.3 pME) Both C) and D) are correct

Enzymes are biological catalysts that help chemical processes occur faster. Enzymes are proteins…

Answered: In your acid phosphatase enzyme…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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For an enzyme following Michaelis-Menten kinetics, the following Vo vs. S data were obtained in steady state experiments using 2 micromolar enzyme for all measurements: [S] Vo 1 mM 4.0 mM/min 2 mM 4.8 mM/min 4 mM 4.9 mm/min 8 mM 4.95 mM/min Estimate the value of kcat for the reaction. Be sure to include the appropriate units.
The commercial sample of carboxyl esterase contained 15.0 mg of enxyme in 0.30 mL of suspension. In your experiment, you add 0.090 mL of this suspension to the sample tube that contains a total volume of 3.0 mL. How many mg of carboxyl esterase enzyme do you have in the sample tube?
If the data from an enzyme experiment is plotted as a Lineweaver-Burk plot, and the Vmax is 0.02 mol/sec, and x-intercept is –2.5 mM then what is the KM value? Show yourwork/reasoning.
Given the initial rate data for the reaction A + B → C, determine the rate expression for the reaction. [A], M [B], M A[C]/At (initial) M/s 0.0418 0.122 2.73 x 10-4 0.0836 0.122 10.9 × 10 4 0.0418 0.488 2.73 x 104 O A[C] At ○ A[C] ΔΙ = 0.439 Ms[A][B]² = 1.27 M²s¹ [A][B] ● A[C] = 6.53 × 10³ s¹ [A] At O A[C] = 0.156 M's¹[A]² At ○ A[C] At = 5.35 x 102 M2s[A][B]
Could you explain step by step how to solve this? I'm not sure how to get all the numbers that are shown in the solved answer.
For an enzyme kinetics experiment, a student prepared a reaction mixture by mixing 450 microliters of 0.75mM PNPP with 4.25ml of 0.2M Tris-HCl buffer. When he is ready to measure the absorbance, he added 0.3ml of Alkaline Phosphatase to the mixture and mixed thoroughly. What is the substrate concentration at the beginning of the reaction in mM ?
8L.16.2
You obtain a calculated Vmax of 4.26uM/s and a Km of 122.5uM from a kinetics experiment performed using 0.5uM enzyme. What is the catalytic efficiency of this enzyme?
If the enzyme lactase has a Vo of 0.40 mM per minute when [S] = 1.25 mM, and a Vo of 1.0 mM per minute when [S] = 5.0 mM, what is its Vmax, Km and the slope on a linewver-burk plot?
make a Gibbs free energy graph as free energy as y-axis a for the transition state as a function of [Gdn HCl] (x-axis) with a line of best fit
You are evaluating the kinetics of an enzyme catalyzed reaction containing 5.5 μM total enzyme and 11.2 μM substrate. At this substrate concentration, you determine that the Vo = 88.6 μmol mL-¹. s-¹. If the Vmax 833.3 mM s the KM is: . == " 30.9 μΜ 10.4 μΜ Ο 124.6 μΜ 234 μΜ 94.5 μM
A purified protein fraction has a total sample volume of 360 µL. The sample has a corrected A280 of 0.484, and the blank corrected A280 was 0.052. (Both values were measured with a path length of 1.00 cm.) If 5.00 µL of the sample was used in a reaction, calculate the mass of protein in the reaction (in µg).

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