7. You want to separate these four proteins in a mixture:Isoelectric pointMol. Weight (kDa)Protein A4.180Protein B9.081Protein C8.837Protein D3.9172Which of the following would be the best order in which to run chromatography columns?A) Anion-exchange at pH 3, then size exclusionB) Cation-exchange at pH 3, then size exclusionC) Cation-exchange at pH 3, then anion-exchange at pH 3D) Anion-exchange at pH 3, then cation-exchange at pH 3E) Size exclusion, then cation-exchange at pH 3F) Size exclusion, then anion-exchange at pH 3

A Physical method for the separation of compounds is called chromatography. In two…

Answered: 7. You want to separate these four…

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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1.) A sample contains 0.003 mg of NaOH. How many micrograms (μg) is this? 2.) An experiment was performed in which 400 mL of 0.2 M urea was used. Calculate the number of millimoles (mmol) of urea contained in this sample. 3.) How many micromoles (μmol) of ATP are present in 4 mL of 5 mM ATP solution..
1. Shown below is the chromatogram for some amino acid standards and two unknowns. Each unknown consists of just a single amino acid. Answer the following questions based on this chromatogram. Solvent Frort Ala Ser Asp Are UrkX Unk Y a) Explain the trend in the distances travelled by the standard amino acids. b) Calculate the R¢values of the standard amino acids and the two unknowns. Show your computations. c) Based on your calculations, what are X and Y? d) Are you able to identify X unambiguously? How about Y? e) If you are unable to identify either one of the unknown amino acids, think of a method by which you can separate them from each other. Explain your answer.
3.) A mixture of amino acids was subjected to paper chromatography with six amino acid standards in order to determine its composition. After visualization using ninhydrin, the measured distances were as follows: A B с D E F G a.) What is the Rf value of each amino acid observed? X Distances: Solvent 10.3cm A 4.50cm B - 1.32cm C - 6.60cm D - 5.20cm E - 3.52cm F 8.70cm G - 10.26cm X1 - 9.72cm X2 - 4.3cm X3 7.1cm - b.) What are the possible components of the amino acid mixture? Answer can be up to two amino acids per component.
Indicate the contrast statements of the following chromatographic techniques of separation. A. A separation of components mixture based on migration rates in a stationary phase by a gaseous or liquid mobile phase. B. The supported materials coated of flat plate or in fibres of paper stationary phase is known as planar chromatography. C. The rate of migration of molecules or analytes is depending on the relative solubility of the solute in the stationary phase and mobile phase. D. Involve an electronic transition of valence shell electron in free atoms to provide analytical information about sample composition.
1.0.1 mL of a protein solution of concentration of 11 mg/mL was diluted to a total volume of 4.0 mL with water (i.e. 0.1 mL of the solution was added to 3.9 mL of water). 2 mL of this solution was then mixed with 18 mL of water. What is the concentration of the diluted protein solution? Space to show your workings:
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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).
A researcher prepares 100 mL of aqueous solution containing 0.1 g of a protein. The researcher then uses an experimental apparatus ,where he notes that, at room temperature (300K) and atmospheric pressure (101.325 kPa), distilled water flows naturally into the solution compartment. However, when he applies an extra pressure of 1000 Pa he observes that the flow of distilled water ceases and the system is in balance. Calculate the molar mass of this protein, in kDa (1 Da = 1 g/ mol); Why does the flow of distilled water cease with the application of the pressure of 1000 Pa? Explain in terms of potential chemicals. %3D
A mixture of proteins contains four different polypeptides, all in ~equal concentration, in solution with the following properties: Protein Molecular Mass (kDa) Isoelectric point A 45 4.5 B 77 6.0 C 28 4.1 D 14 10.7 A fraction of the protein solution is applied to a strong cation exchange column using a buffer at pH 8.0 with increasing [NaCl] from 0.05 M – 1.0 M. The chromatogram is shown below: 1. Based on the data presented, which of the following statements is true: Peak #1 is protein D Peak #4 is protein C Peak #3 is protein A Peak #4 is protein D Peak #2 is protein B 2. Since you know that the proteins are all present in approximately equal concentrations, the different relative peak areas tell you that: There are more neutral amino acids in protein #4…
2.) An unknown amino acid was subjected to paper chromatography with five amino acid standards in order to identify it. After visualization using ninhydrin, the distances travelled were measured as follows: A B с D E X Distances: Solvent - 9.3cm A - 1.33cm B - 4.75cm C - 2.44cm D - 7.62cm E - 8.75cm X - 1.45cm a.) What is the Rf value of each amino acid sample? b.) Arrange the amino acids from most non-polar to least non-polar (include sample X). c.) What is the possible identity of the unknown amino acid? Answer can be up to two amino acids.
An ion-exchange chromatographic separation is performed using a diethyl-aminoethyl- (DEAE)-sepharose column to separate proteins in a mixture. The mixture contains Protein A (pl=6.0), B (pl35.0), C (pl=7.5), D (pl =1), and E (pl=4.0). The protein mixture is prepared in a buffer solution pH =5. When the protein mixture is loaded onto the column, and the column is washed with a buffer solution pH 5, which protein(s) will be captured by DEAE-sepharose in the column? O Protein B because it is predominantly in net negative charge form. O Proteins D and E because they have predominately net negative charge in pH 5 solution O Proteins A, C, D and E because they have charges O Proteins A and C because both both predominantly have net positive charges O Proteins Band E because both predominantly have net positive charges
A solution contains a mixture of four proteins: urease, ovalbumin, lysozyme, and alkaline phosphatase. The proteins have the following properties. Molecular weight (Daltons) Protein pl Urease 483,000 5.0 Ovalbumin 45,000 4.6 Lysozyme 86,000 11.0 Alkaline 86,000 4.6 Phosphatase Based on the information provided, what type of chromatography (gel permeation or ion exchange) could be used to separate: a) Lysozyme from Alkaline Phosphatase. Briefly explain your answer. b) Ovalbumin from Alkaline Phosphatase. Briefly explain your answer. c) Which of the four proteins would be bound to a cation exchanger equilibrated at pH 5? d) Briefly explain your answer to part c).

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