Composition of Cell Lysis Buffer Volume or Weight of Reagents Needed Required Concentration of Reagent Molecular Weight 40 mM Tris HCI 20 mM Acetic acid 157.59 60.05 1 mM EDTA 292.24 10 mM MgCl2 from 25mM stock 5% SDS ddH20 95.21 288.37 18.02
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In this experiment, you are to prepare 250mL of Cell Lysis Buffer using the reagents given in Table. Fill out the table. Show your computations at the bottom of the table.
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- Composition of Cell Lysis Buffer Required Concentration of Reagent Molecular Weight Volume or Weight of Reagents Needed 40 mM Tris HCl 157.59 20 mM Acetic acid 60.05 1 mM EDTA 292.24 10 mM MgCl2 from 25mM stock 95.21 5% SDS 288.37 ddH2O 18.02The diffusivity of amino acids in polyacrylamide gel is approximately 1x10^-9 cm2./s calculate the initial flux of amino acids, give an instantaneous gradient of (20g/cm 3 )/8cm Why is polyacrylamide gel is used in electrophoresis?Infuse heparin at 1,200 units per hour from a solution containing 40,000 units of heparin in 500 mL D5W. How many mL/hr will deliver the ordered dosage?
- The isoelectric point of eIF4a is 5.02. Students are given a sample of cell lysate containing eIF4A at pH 7.4. They are also provided with two buffers of pH 7.4 to use for ion exchange chromatography. One buffer has a very high salt concentration (1 M), the other has a low salt concentration (0.1 M). Mariela decides to use an anion exchange column, while Ashok chooses a cation exchange column. Who made the better decision? Provide a detailed explanation of why one student will end up with a purer sample of eIF4A. Which buffer will you use while washing away impurities (high or low salt), and which would you use to remove eIF4A from the column? Explain your choice.after a 5 g onion sample is divided into two equal parts, heat treatment to one of these partsit is being implemented. Then both heat-treated and non-treated parts are 10 times their weightit is ground in an environment containing as much buffer and the determination of pyruvate in the supernatants obtainedit's being done.a) As a result of measurements taken at 520 nm; absorbance value for the heat-treated sample;it was found that the absorbance value in the sample that was not heat treated was 0.123 and the absorbance value in the sample that was not heat treated was 0.520.The equation of the calibration accuracy for pyruvate is that y = 0.1367x – 0.001 (nmol/mL)according to the onion sample; a) independent of alinase activity; b) dependent on alinase activityand c) calculate the total pyruvate amounts in terms of nmol/g of onion.b) How is there a relationship between the activity of the enzyme allinase in onions and the amount of pyruvate?Dec,please explain.Show the calculations required to make up 250mlof a stock solution of this chemical that will then be at the working concentration when 1 volume of this solution is added to 10 volumes of cell culture medium.
- what is the concetration of a lysozyme solution with an absorbance of 0.720 measured at 280 nm( e= 36000 -1M -1cm,l=1cm)A glucose solution is supplied in a repeated fed batch culture. The following parameters have been measured at t=2.5 hours; the system was under a quasi-steady state at this time. V = 1.0L, F = 0.22L/hr, S_0 = 98g/L, mu_m = 0.31/hr, K_s = 0.14 g-glucose/L, YM_X/S = 0.48 g-cells/g-glucose, Xt_0 = 33g (1) Calculate the value of V0 and S. (2) Calculate the value of Xt for t = 2.5hrs.Calculation at the initial point of a complexation titration: What is the pSr value of a 50.00 mL solution of 0.01000 M Sr2+ (formation constant, Kf = 5.348 x 108) after the addition of 0.00 mL of 0.02000 M EDTA which was buffered to pH 11.00? Round your final answer to two decimal places to the right of the decimal point.
- Dextrose 5% in water solution is an example of hypertonic solution. True False?The octapeptide gly-cys-met-asn-lys-ala-tyr-gly was hydrolyzed consecutively by CNBr and then trypsin (3 fragments total). The mixture of fragments was buffered at a pH 8.5 and then chromatographed on an anion-exchanger (positive resin) with the same buffer. Draw sequence (abbreviated form) of all fragments at that pH (show charges) and predict elution order.The protein calcineurin binds to the protein calmodulin with an association rate of 8.9 × 103 M−1 s −1 and an overall dissociation constant, Kd, of 10 nM. Calculate the dissociation rate, kd , including appropriate units.