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  • Title: Two alpha-chain hemoglobin variants, Hb Broussais and Hb Cemenelum, characterized by cation-exchange HPLC, isoelectric focusing, and peptide sequencing.
    Author: Turpeinen U, Sipilä I, Anttila P, Karjalainen U, Kuronen B, Kalkkinen N, Ahola T, Stenman UH.
    Journal: Clin Chem; 1995 Apr; 41(4):532-6. PubMed ID: 7720241.
    Abstract:
    We here report the characteristics of two rare alpha-chain hemoglobin (Hb) variants. The variants were found during quantification of HbA1c 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-->Asn] and Hb Cemenelum [alpha 92 (FG4)Arg-->Trp].
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