The Primary Structure of the Constant Part of μ-Chain-Disease Protein BOT

Human IgM Polymorphism

Authors

  • Edith MIHAESCO,

    1. Groupe de Recherches d'Immunochimie et d'Immunopathologie (Unité 108 de I'Institut National de la Santé et de la Recherche Médicale), Unité d'hseignement et de Recherche d'Hématologie, Centre Georges-Hayem, Hôpital Saint-Louis, 2 Place du Docteur-Fournier, F-75475 Paris-Cedex-10, France
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  • Shitsu BARNIKOL-WATANABE,

    1. Max-Planck-Institut für Experimentelle Medizin, Hermann-Rein-Straße 3, D-3400 Göttingen, Federal Republic of Germany
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  • Heinz Ulrich BARNIKOL,

    1. Max-Planck-Institut für Experimentelle Medizin, Hermann-Rein-Straße 3, D-3400 Göttingen, Federal Republic of Germany
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  • Constantin MIHAESCO,

    1. Groupe de Recherches d'Immunochimie et d'Immunopathologie (Unité 108 de I'Institut National de la Santé et de la Recherche Médicale), Unité d'hseignement et de Recherche d'Hématologie, Centre Georges-Hayem, Hôpital Saint-Louis, 2 Place du Docteur-Fournier, F-75475 Paris-Cedex-10, France
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  • Norbert HILSCHMANN

    1. Max-Planck-Institut für Experimentelle Medizin, Hermann-Rein-Straße 3, D-3400 Göttingen, Federal Republic of Germany
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Abstract

The complete primary structure of the constant part of the u-chain-disease protein, BOT, was established. It includes the whole CH2, CH3 and CH4 domains. Two amino acid changes were found, at positions 309 (Ser→Gly) and 333 (Val→ Gly) (GAL numbering). In two additional monoclonal μ chains (SCO and CO), the same positions showed an amino acid variability. From these data it may be concluded that four types of μ chains exist in the human: (1) GAL type with Ser-309 and Val-333; (2) OU type with Gly-309 and Val-333; (3) SCO type with Ser-309 and Gly-333; (4) BOT/CO type with Gly-309 and Gly-333. The meaning of this molecular polymorphism is discussed.

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