You hope to separate Pca from at least two of the proteins in the mixture by anion exchange chromatography. Which condition(s) would allow you to do that?
A. You boil the protein solution before loading the protein onto the column.
B. You bring the NaCl concentration of the protein mixture to 200 mM before loading.
C. You increase the flow-rate of the elution buffer through the column from 1 to 5 ml/min.
D. You load the protein mixture in a solution without NaCl and then wash the column with a solution containing 800 m NaCl.
One of your co-workers suggests another method: changing the pH of the elution buffer. In the original chromatography, the pH of the elution buffer is 7.5.
Which two of the following statements are correct?
A. The isoelectric point of a protein is the pka of the amino acid that is equidistant from the amino and carboxy termini of a protein.
B. In a solution whose pH equals the isoelectric point of a protein, the net charge of the protein is 0.
C. In a solution whose pH is higher than the isoelectric point of a protein, the net charge of the protein is negative.
D. In a solution whose pH is lower than the isoelectric point of a protein, the net charge of the protein is negative