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  • Title: Characterization of a new electrophoretically silent hemoglobin variant. Hb saale OR alpha 2beta 2 84(EF8)Thr --> Ala.
    Author: Bissé E, Zorn N, Heinrichs I, Eigel A, Van Dorsselaer A, Wieland H, Kister J, Marden MC.
    Journal: J Biol Chem; 2000 Jul 14; 275(28):21380-4. PubMed ID: 10770934.
    Abstract:
    A new abnormal hemoglobin was detected in a young German anemic patient by cation-exchange high performance liquid chromatography (HPLC). Using a combination of electrospray mass spectrometry, HPLC, direct sequencing, and family screening with polymerase chain reaction/restriction digestion approach, we have characterized this hemoglobin variant as resulting from a Thr --> Ala replacement at beta84(EF8). It could be separated neither by electrophoresis nor by isoelectric focusing. Hb Saale is slightly unstable, exhibiting a moderate tendency to auto-oxidize. Functional properties and the heterotropic interactions are similar to those of Hb A.
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