Two alpha-chain hemoglobin variants, Hb Broussais and Hb Cemenelum, characterized by cation-exchange HPLC, isoelectric focusing, and peptide sequencing

Turpeinen, U.; Sipilä, I.; Anttila, P.; Karjalainen, U.; Kuronen, B.; Kalkkinen, N.; Ahola, T.; Stenman, U.H.; Turpeinen, U; Sipilä, I; Anttila, P; Karjalainen, U; Kuronen, B; Kalkkinen, N; Ahola, T; Stenman, U.H

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Two alpha-chain hemoglobin variants, Hb Broussais and Hb Cemenelum, characterized by cation-exchange HPLC, isoelectric focusing, and peptide sequencing

Turpeinen, U.; Sipilä, I.; Anttila, P.; Karjalainen, U.; Kuronen, B.; Kalkkinen, N.; Ahola, T.; Stenman, U.H.

Clinical Chemistry 41(4): 532-536

1995

ISSN/ISBN: 0009-9147

PMID: 7720241

Document Number: 450119

We here report the characteristics of two rare alpha-chain hemoglobin (Hb) variants. The variants were found during quantification of HbA-1c by cation-exchange HPLC with the Diamat glycohemoglobin analyzer. They were further characterized by isoelectric focusing and PolyCAT A cation-exchange chromatography. The structure of the abnormal Hbs was established by amino acid analysis after separation of the globin chains by reversed-phase chromatography, digestion with trypsin, separation of the peptides by reversed-phase chromatography, and amino acid sequencing. These studies showed that the two variants were Hb Broussais (alpha-90 (FG2)Lys fwdarw Asn) and Hb Cemenelum (alpha 92 (FG4)Arg fwdarw Trp).