What's your next step to characterize this enzyme?
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![6. You are officially in beast-mode. Your thesis deadline is coming up and you are
purifying enzymes like crazy and testing their kinetics. You get the following data for
one of your enzymes.
[S] (µM)
0
1
2.5
5
10
20
50
100
V. (μm/sec)
0
18
46
105
195
450
1218
1841
What's your next step to characterize this enzyme?](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F424482ac-ef50-4214-a1e3-aaaeb325792a%2Fc0769efa-44e6-49e8-a1d2-d2d99d756080%2Fhmk7v4_processed.png&w=3840&q=75)
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- Concentrations in biochemical systems are often very dilute. Consequently, scientific notation and logarithms are often used to express concentrations. In scientific notation, numbers are expressed as coefficient x 10" To convert a number to scientific notation, proceed as follows: 1. Move the decimal place so that there is one digit in front of the decimal. 2. Account for the moved decimal in the value of x. If the decimal moved to the right, x is negative; if it moved to the left, x is positive. A logarithm is basically an exponent. Unless otherwise indicated, a logarithm is the a of 10". The numbers after the decimal point are significant; the number before the decimal just identify the location of the decimal point for the number. Notice that it is easy to estimate a logarithm from scientific notation; it's the exponent! Logarithms are commonly used to express the concentration of H. The pH is defined as pH= log (In), where the base number is 2.303. The same general rules as logs…A purified protein sample was used in a reaction, resulting in an activity of 696.7 nmol min-1. The reaction volume was 145.0 µL and the final volume before loading the plate was 1,050 µL. The total reaction time was 4.25 min. The amount of protein used in the reaction was 4.270 µg. Calculate the specific activity of the sample (in nmol min-1 µg-1).You are interested in purifying an enzyme X and decide to use an affinity chromatography followed by an enzymatic assay. You obtain the following data: Total volume of [protein] the sample (ml) (mg/mL) (U) |Total activity Sample name Specific activity |(U/mg) |Affinity | chromatography 2 0.12 5000 20833 You have obtained a 10X fold purification and a yield of 10% at the Affinity step. What was the protein concentration of your crude lysate sample, if its volume was 15 mL? Detail your answer by showing the calculations, and do not forget the UNITS!
- 8 7- 6- 2- 1- 45 90 135 180 225 270 315 360 405 450 495 540 58! [Substrate] (nM) What is the Vmax of the enzyme data shown above? rate (nM/sec) 3.Give a complete and well descriptive definition of the following:1.1 Enzyme catalysis1.2 Co-enzyme1.3 Negative heterotropic co-cooperativitA technician prepares a buffer solution that will be used to facilitate the optimal pH for an enzyme involved in the biotechnological degradation of organic compounds. The buffer compound will facilitate a stable pH. To prepare the buffer they need to determine the required concentration of anita hara [conjugate acid or base]_08 They have been provided with the buffer parameters provided in the images. Provide the answer to three decimal places and include an appropriate unit. Note: You may need to round the numbers to get the required answer. Final volume of solution: 200 ml VEENER Total buffer compound concentration: 150 mM Ratio conjugate base/weak acid: 1.58/1 2000 Concentration weak acid: 0.058 M Final pH of solution: 6.5 Buffer compound pk.: 6.3 14 13 12 11 10 9
- How many net molecules of nucleoside triphosphate (ATP and equivalent molecules) are produced by complete aerobic catabolism of a glucose going through glycolysis, the pyruvate dehydrogenase complex and the citric acid cycle (TCA cycle)? Do not count the ATP eventually generated by re-oxidation of reduced coenzymes, just the number of NTPs produced in reactions of these pathways. Choose the one best answer. 02 03 04 05 06 8A biochemist discovers and purifies a new enzyme, generating the purification table below. Procedure Total Protein (Mg) Activity (Units) Crude Extract 20,000 4,000,000 Precipitation (Salt) 5,000 3,000,000 Precipitation (pH) 4,000 1,000,000 Ion Exchange Chromatography 200 800,000 Affinity Chromatography 50 750,000 Size-exclusion Chromatography 45 675,000 a) From the information given in the table, calculate the specific activity of the enzymeafter each purification procedure.b) Which of the purification procedures used for this enzyme is most effective (i.e., givesthe greatest relative…If 287.9 umol of enzyme X has a Vmax = 47.8 mmol/sec, what is the value of kcat %3D sec-1? Please report answer with 1 decimal place. Please do not report units. Your Answer: Answer units MacBook Air 888 F5 F4 F3 F2 %23 %24 %24
- You are working on an enzyme that obeys standard Michaelis-Menten kinetics. What variable is the V, dependant on if the concentration of the substrate is substantially higher than the concentration of the enzyme? [S] [E] [ES] O [P] O not enough information providedMike has determined that enzyme he is attempting to purify has an isoelectric point of 4.5 (pI = 4.5). He has decided to examine anion exchange chromatography as a potential purification step. He tested out using 2 different buffer and linear NaCl gradient on HPLC (like what you did). His results are shown below. Which buffer should Mike uses for his purification (both buffer has pH higher than enzyme’s pI)? Why?Enzyme A catalyzes the reaction S → P and has a KM of 50 μM and a Vmax of 100 nM s–1. EnzymeB catalyzes the reaction S → Q and has a KM of 5 mM and a Vmax of 120 nM s–1. When 100 μM ofS is added to a mixture containing equal amounts of enzymes A and B, which reaction product (Por Q) will be more abundant after 1 minute of reaction?
