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Abstract
Amino acid analysis of 2-aminoethylphosphonic acid (2-AEP) under the conditions normally used for the analysis of acidic amino acids in protein hydrolysates resulted in the elution of 2-AEP as two incompletely resolved peaks. Evidence is provided indicating that this phenomenon was due to the formation of a degradation product or an isomer on the ion-exchange column and that the resin, buffer pH and column temperature were all contributory factors.
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