Normally in chromatography, the eluent strength increases with increasing salt c

Question

Normally in chromatography, the eluent strength increases with increasing salt concentration. However, in hydrophobic interaction chromatography, commonly used to separate proteins, the opposite is true: eluent strength increases when the salt concentration decreases in the eluent. Why?

A) Less concentrated eluent induces more interaction between the protein and the hydrophobic stationary phase, allowing the protein to be removed from the column with greater ease

B) After a protein has been bound onto the column with a high salt concentration, an eluent with a gradient range of decreasing salt concentration is added, since lower salt concentration increases the solubility of protein in water.

C) High concentrations of salt in the eluent cause the proteins to "salt out" of solution, making them unable to bind to the stationary phase of the column

D)None of the above.

Explanation / Answer

Answer B

After a protein has been bound onto the column with a high salt concentration, an eluent with a gradient range of decreasing salt concentration is added, since lower salt concentration increases the solubility of protein in water.

Related Questions

Navigate

• Browse (All)
• Browse N
• Subjects

Integrity-first tutoring: explanations and feedback only — we do not complete graded work. Learn more.