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Biochemistry · Biomolecules and enzymes: cation-exchange chromatography of amino acids
Sample itemA mixture of alanine, aspartate, glutamate and lysine at pH 7 is loaded onto a cation-exchange resin that carries negatively charged groups. The column is then eluted with increasing salt concentration. Which amino acid emerges last?
Original practice item, not a recalled exam question. Nothing here is recorded.
The answer and the reasoning
A. Lysine
A cation-exchange resin binds positively charged molecules. At pH 7 lysine carries a net positive charge, so it sticks most tightly and is displaced last. Aspartate and glutamate are negatively charged and are repelled, so they run through first, and alanine is a neutral zwitterion that elutes in between.
Option by option
A. Lysine (correct)
Correct. Lysine is the only amino acid with a net positive charge at pH 7, so it binds the resin most strongly.
B. Glutamate
Glutamate is negatively charged at pH 7 and is repelled by the resin.
C. Aspartate
Aspartate is negatively charged at pH 7 and is repelled by the resin.
D. Alanine
Alanine has no net charge at pH 7 and is not retained by electrostatic attraction.
Source note: Original NextPrep sample item — pending expert review. This item is original practice material awaiting independent expert review, so confirm important facts in a standard textbook.
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