Abstract
The present article describes a simple and rapid new peptide mapping procedure that could be used to assist identification of rare hemoglobin variants in clinical laboratories. Four hemoglobin variants were taken as example, namely Hb D-Ouled Rabah, Hb Marseille, Hb G-Philadelphia, and Hb Ube-2, and isolated by electrophoresis at alkaline pH. The globin chains were aminoethylated and, after tryptic digestion, the peptides were separated by a capillary zone electrophoresis method. Highly reproducible migration times of the peptides were obtained with intra-assay and inter-assay coefficients of variation of less than 1 and 2%, respectively.
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