In order to separate protein X using ion exchange chromatography, I am using a resin with Schiff nitrogens attached (pKa is 6.0), If I wanted to separate protein X, whose pl is 7.0, what is the pH range of the buffer that can be used for ion exchange chromatography with this resin? there is no pH range for this resin and protein X. O any pH above 6.0. ) any pH between 6.0 and 7.0 any pH below 7.0

In order to separate protein X using ion exchange chromatography, I am using a resin with Schiff nitrogens attached (pKa is 6.0), If I wanted to separate protein X, whose pl is 7.0, what is the pH range of the buffer that can be used for ion exchange chromatography with this resin? there is no pH range for this resin and protein X. O any pH above 6.0. ) any pH between 6.0 and 7.0 any pH below 7.0

Chemistry

10th Edition

ISBN:9781305957404

Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Chapter1: Chemical Foundations

Section: Chapter Questions

Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...

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23-24 A 1.013-g sample of tuna was analyzed by the Kjeldahl method. The ammonia formed was distilled into a 75.00-mL 0.02139 M H₂SO₄ solution. A 5.21 mL back-titration of 0.05324 M NaOH was required. (Note the stoichiometry of your acid and base) QUESTION.a) What is the % N (14.007 g/mol) of the tuna sample? b) If fish in general has 5.71 g protein per g N, what is the % protein of the sample?
titrimetric profile of lysine
Aliquots of a 0.5 mg/mL standard of BSA were used to construct a standard curve for the Bradford protein assay. The tubes contained the following amounts of the BSA solution: 0, 20, 40, 60, 80, 100 μL. Each sample then had water added to make the final volume 100 μL. The corresponding absorbencies after adding Bradford reagent were the following: 0, 0.05, 0.09, 0.14, 0.19, and 0.22. If you took 20 μL of an unknown and added 80 μL of water, mixed, took 10 μL of the mixture and 90 μL of water and added the Bradford reagent and saw an absorbance of 0.08, what was the protein concentration of the undiluted unknown to one decimal place?
Briefly explain the principle behind the following techniques:(a) ion-exchange chromatography (b) gel filtration chromatography (c) affinity chromatography (d) Use three diagrams to illustrate the separation of three different proteins by thesemethods.
You need to separate a mixture of dyes on an agarose gel. You have been provided with 5X TAE (Tris acetate buffer) The electrophoresis tank needs 250 ml of buffer and the gel volume required is 50 ml. Show calculations for making 1X TAE gel running buffer and 1.25% agarose gel for your experiment. Explain how you will prepare the buffer and gel 4m
A fish sample was analyzed for crude protein content using the Kjeldahl method. Thefollowing data were recorded: Moisture content 10.0%Weight of sample 2.15 gNormality of HCl used for titration 0.121 NHCl used for sample 28.5 mLHCl used for reagent blank 0.2 mL Calculate crude protein content on wet weight basis of the fish sample, assuming fishprotein contains 20% nitrogen.
A Na2S2O3 titrant was standardized by taking 50.0 mL of 6.7863 x 10-3 M standard KIO3 solution, acidifying, and adding KI crystals. Titration of this solution required 9.80mL to reach the starch endpoint. What is the concentration of the Na2S2O3 titrant?
Beginning at pH=pI you titrate 15mL of a 0.2M tetrapeptide Lys-Arg-His-Glu with 30mL of a 0.25M HCl. What is the final pH of the solution? (Relevant pKa values are: 2.2, 4.2, 6.0, 9.6, 10.5, and 12.5). At pH 9.7, would the predominant form of the tetrapeptide bind a cation exchange column, anion exchange column, or neither? In 1 sentence explain your answer.
Calculate the pH at each of the following points for the titration of 100 mL of 0. 6 M dl-Histidine with the following volumes of 1.20 M sodium hydroxide. H3His ↔ H+ + H2His- Ka1 = 3.98x10-3 H2His- ↔ H+ + HHis2- Ka2 = 9.12x10-7 HHis2- ↔ H+ + His3- Ka3 = 4.67x10-10 Vol. of NaOH Calculated pH 0 mL 30 mL 50 mL 75 mL 100 mL 125 mL 135 mL 150 mL 175 mL Please provide a sketch of the titration curve and label both the x & y axis and applicable equations used at each data point (e.g., pH = - log[H+] or pH = pKa or pH = pKa + log )
Protein ABC is a heme-containing protein responsible in electron transfer in microalgae. The target protein was extracted using ammonium sulfate fractional precipitation and quantified using Bradford assay. A set of solutions with increasing concentration was prepared using 15.00 mg/mL analogous protein standard [refer to succeeding table]. Each solution was treated with 80 μL of Bradford reagent and diluted to 1.500mL. The absorbance at 595 nm of each solution was obtained and presented below. Volume of protein std, μL A595 0 0.0002 10 0.0007 25 0.0075 50 0.0165 100 0.0356 250 0.0930 500 0.1950 750 0.3010 1000 0.4175 Report the equation of the calibration curve and proof of linearity (R2 value).
1) What causes the components in a misture to separate in a chromatography experiment like Paper Chromatography of Metal Ions? 2) The lower the detection limit of a particular analyical method, the more sensitive the method. Explain. 3) You will prepare teo sheets of chromatography paper in Paper Chromatography of Metal Ions experiment. How many solutions will be applied to piece of paper? Why can't all six spots be placed on one sheet? Exaplin.
21-22.A 0.2119-g of primary-standard grade Na₂CO₃ (106.00g/mol) was treated with 50.00 mL of HClO₄ solution. After boiling to remove CO₂, it was back-titrated with 10.28 mL of NaOH solution to neutralize the excess HClO₄. In a different experiment, 29.34 mL of the HClO₄ solution neutralized a 25.00-mL portion of the NaOH solution. (Note the stoichiometry of your acid and primary standard).QUESTION. a.) What is the concentration of the HClO₄ solution? b.) What is the concentration of the NaOH solution?