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J. Biol. Chem., Vol. 275, Issue 28, 21380-21384, July 14, 2000

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Characterization of a New Electrophoretically Silent Hemoglobin Variant
Hb Saale OR ₂₂ 84(EF8)Thr  Ala^*

Emmanuel Bissé^§, Nathalie Zorn^¶, Irene Heinrichs, Antonin Eigel^**, Alain Van Dorsselaer^¶, Heinrich Wieland, Jean Kister, and Michael C. Marden

From the  Department of Clinical Chemistry, University Hospital, Hugstetterstrasse 55, D-79106 Freiburg, Germany, the ^¶ Laboratoire de Spectrometrie de Masse Bio-Organique URA31, CNRS Université Louis Pasteur, Faculté de Chimie, F-67008 Strasbourg, France, the  Division of Pediatrics, Martin-Luther-Universität, D-06097 Halle, Germany, the ^** Institut für Humangenetik Westfälische Wilhelms-Universität, D-48149 Münster, Germany, and the  INSERM U473, 94276 Le Kremlin Bicêtre, France

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 84(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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