You need to make a 10 ng/ul solution of enzyme from a 100 mg/ml solution. How will you use a dilution series to do this? You should not pipette less than 1 ul. Any dilutions made need to be 5 ml in volume.
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- As an intermediate step in making the enzyme solution, you need to prepare Buffer X using the stock solutions of each chemical. Describe how you would make 100 mL of buffer X that has the following concentrations and pH: 50mM NaCl, 20mM Tris, 5mM MgCl2, pH 7.5 You do this starting with stock solutions of 1M NaCl, 1M Tris, 1M MgCl2, and water and a pH meter.A continuous enzyme reactor consists of a stirred tank of volume 0.01 m3 through which liquid is pumped at 0.02 m3⁄h. The enzyme is immobilised onto non-porous, spherical support particles, and the contents are stirred well to ensure that the composition is uniform and that the particles remain in suspension. A plastic mesh has been placed in front of the exit pipe to prevent the particles from leaving the vessel. The reactor is used to carried out a 98% conversion of a substrate entering at 0.1 kmol m3 ⁄ . Michaelis-Menten kinetics apply, with the following enzyme characteristics: Turnover number = 1 × 10^3 s KM = 5 × 10−3 kmol m3 ⁄ Enzyme RMM = 65,000 (a) If the enzyme is stable, calculate the mass of enzyme that needs to be immobilised. (b) If the enzyme is not stable and experiences exponential denaturation with a half-life of 10 h at the reaction temperature, determine the denaturation constant. (c) How would you expect denaturation to affect the reactor performance?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).
- Which of the following statements regarding size exclusion chromatography is false? During size exclusion chromatography, the largest compounds elute out first. The elution order of fully excluded compounds follows an inverse diagonal relationship with respect to elution volume. During size exclusion chromatography, the smallest compounds elute out at the end. The elution order of partially included compounds follows an inverse diagonal relationship with respect to elution volume. While performing enzyme kinetics, you mixed 100 μL of Carb 1 sample to 2.9 mL bacteria, and got a reading of [Abs/min] equal to 0.5. Calculate the total activity in your carb 1 sample, if the total volume is 15 mL and the sample was undiluted. 7500 activity units 750 activity units 7.5 activity units 75 activity unitsYou run a series of assays at 25°C on enzyme A. You measure the velocity for a range of S concentrations. What is the Km (in mM) for Enzyme A?Calculate your dilution strategyto make a 625 ng/mLHRP solution from a 12.5 μg/mL stock given the totalvolume of enzyme youwillneed for your condition this week. Note if you are testing pH, you only need to calculate one enzyme dilution because all other pHs will use the same strategy.
- An enzymatic reaction follows M-M kinetics with Vmax= 2.5 mol m-3s-1and Km = 5 mM.Calculate the time required for 50% conversion of the substrate in a batch reactor if theinitial substrate concentration is0.2 M.Show your calculation steps.An experiment on enzyme-catalyzed reaction was conducted in the laboratory by a student. Results obtained are summarized in the table below. In all the experiments, the concentration of the enzyme is the same. Substrate Concentration Velocity (pmol) (pmol/min) 1.5 0.21 0.28 4 0.32 6 0.36 0.4 15 0.45 18 0.47 1. Plot or graph these results using the Lineweaver-Burk method. 2. Determine the Km and Vmax values. Show all equations and calculations.You put 50 uL of 0.1 mg of protein into a 1 cm pathlength cuvette containing 3 mL of LDH reaction mixture and measure a slope of 0.125 abs/min in an LDH assay. What is the specific activity of the enzyme sample? Show your work.
- What is the parameter in the enzyme measurements?An enzyme-catalyzed reaction has a Km of 4 mM and a Vmax of 5x10-3 uM/s. What is the reaction velocity when the substrate concentration is: 5 mM 4 mMA 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