Write down the values in bold print. You are isolating a protein with a pl of 8.5 using cation exchange chromatography. You add your protein to the column in a solution at pH of 3 and collect the eluant as fraction A. You then wash the column with a buffer at pH 5 and collect the eluant as fraction B. You do a third wash of your column with buffer at pH of 7 and collect the eluant as fraction C. You do a fourth and final wash of the column with buffer at pH 12 and collect the eluant as fraction D. Which fraction contains most of your protein? O Fraction A O Fraction B O Fraction C O Fraction D O None of the above O All of the above

Write down the values in bold print. You are isolating a protein with a pl of 8.5 using cation exchange chromatography. You add your protein to the column in a solution at pH of 3 and collect the eluant as fraction A. You then wash the column with a buffer at pH 5 and collect the eluant as fraction B. You do a third wash of your column with buffer at pH of 7 and collect the eluant as fraction C. You do a fourth and final wash of the column with buffer at pH 12 and collect the eluant as fraction D. Which fraction contains most of your protein? O Fraction A O Fraction B O Fraction C O Fraction D O None of the above O All of the above

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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The following stock solutions are available to make a protein extraction buffer: 100% Nonidet P-40, 1 M Tris-Cl, and 0.5 M EDTA. What quantity of the original stocks will be needed to make 250 ml of buffer with the following final concentrations: 0.5% Nonidet, 150 mM Tris-Cl, and 10 mM EDTA?
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
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