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Complete Nucleotide Sequence of a Hemoglobin Gene Cluster from the Midge Chironomus thummi piger

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Structure and Function of Invertebrate Oxygen Carriers

Abstract

The aquatic larvae of non-biting midges (Chironomidae, Diptera) contain a variety of Hb proteins in their hemolymph that enable them to survive in an anoxic environment (1). In Chironomus thummi thummi, 12 different Hb variants have been identified and their amino acid sequences determined (2). Based on these primary structures, the evolutionary relationships between the five monomeric and the s e v e n dimeric Hb proteins have been deduced (2). The two groups are thought to have evolved in two different lineages which separated more than 255 million years ago.

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Author information

Authors and Affiliations

  1. Institute of Genetics, Johannes Gutenberg University, Beeherweg 32, 6500, Mainz, Federal Republic of Germany

    T. Hankeln, P. Rozynek & E. R. Schmidt

  2. Institute of Genetics, Ruhr University, Universitätsstrasse 150, 4630, Bochum 1, Federal Republic of Germany

    C. Luther

Authors
  1. T. Hankeln
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  2. C. Luther
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  3. P. Rozynek
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  4. E. R. Schmidt
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Editor information

Editors and Affiliations

  1. Biochemistry Department, Wayne State University School of Medicine, Detroit, MI, 48201, USA

    Serge N. Vinogradov

  2. Enrico Fermi Institute, University of Chicago, Chicago, IL, 60637, USA

    Oscar H. Kapp

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© 1991 Springer-Verlag New York, Inc.

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Hankeln, T., Luther, C., Rozynek, P., Schmidt, E.R. (1991). Complete Nucleotide Sequence of a Hemoglobin Gene Cluster from the Midge Chironomus thummi piger . In: Vinogradov, S.N., Kapp, O.H. (eds) Structure and Function of Invertebrate Oxygen Carriers. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-3174-5_39

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  • DOI: https://doi.org/10.1007/978-1-4612-3174-5_39

  • Publisher Name: Springer, New York, NY

  • Print ISBN: 978-1-4612-7825-2

  • Online ISBN: 978-1-4612-3174-5

  • eBook Packages: Springer Book Archive

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