Could capillary zone electrophoresis of tryptic peptides be used for the characterization of hemoglobin variants?
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.
Lin
C
C
Department of Clinical Chemistry, Hĵpital Erasme, Brussels, Belgium.
Gulbis
B
B
Delobbe
E
E
Robberecht
P
P
Cotton
F
F
Fontaine
B
B
Vertongen
F
F
D000595:Amino Acid Sequence; D019075:Electrophoresis, Capillary; D014644:Genetic Variation; D005914:Globins / Q000032:analysis / Q000378:metabolism; D006455:Hemoglobins, Abnormal / Q000032:analysis* / Q000378:metabolism; D006801:Humans; D010446:Peptide Fragments / Q000737:chemistry; D010449:Peptide Mapping / Q000379:methods*; D015203:Reproducibility of Results; D014357:Trypsin / Q000378:metabolism
D006455:Hemoglobins, Abnormal; D010446:Peptide Fragments; C056357:hemoglobin D Ouled Rabah; D005914:Globins; C031679:hemoglobin G Philadelphia; C033431:hemoglobin UBE-2; C044001:hemoglobin Marseille; D014357:Trypsin