In anion-exchange chromatography, is the resin positively or negatively charged?

Question

In anion-exchange chromatography, is the resin positively or negatively charged? And therefore, overall, should what you want to bind to the column be positively or negatively charged?

Select one:

a. Resin negative; analyte positive

b. Resin positive; analyte positive

c. Resin positive; analyte negative

d. Resin negative; analyte negative

Bound proteins are eluted from a hydrophobic interaction column by increasing or decreasing the salt concentration?

Select one:

a. Increasing

b. Decreasing

The pI of a protein is the isoelectric point, where, on average, the positive and negative charges are equal. To ensure an overall negative charge, a buffer should be used that maintains the pH of the protein containing solution 1 unit above or below the pI of the protein being purified?

Select one:

a. Below

b. Above

How can proteins be eluted from an anion-exchange column?

Select one or more:

a. Decreasing ionic strength

b. Increasing ionic strength

c. Changing the pH

Explanation / Answer

c) In anion exchange chromatography, the resin contains positive charge whereas the analyte negatively charged. b) decreasing salt concentration will lead to increased elution. b) for the overall negative charge in the buffer, pH>pI. B) and C)  increasing the ionic strength by increasing salt concentration and changing pH can help protein be eluted from an anion exchange column.

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