Journal of Molecular Evolution

, Volume 40, Issue 6, pp 663–670

Sequence analysis and structural features of the largest known protamine isolated from the sperm of the archaeogastropod Monodonta turbinata

Authors

  • M. Daban
    • Department d'Enginyería Química, ETSEIBUniversitat Politècnica de Catalunya
  • A. Martinage
    • URA, CNRS 1309, Chimie des BiomoléculesInstitut Pasteur
  • M. Kouach
    • URA, CNRS 1309, Chimie des BiomoléculesInstitut Pasteur
  • M. Chiva
    • Department d'Enginyería Química, ETSEIBUniversitat Politècnica de Catalunya
    • Department de Ciències Fisiològiques Humanes i de la NutricióUniversitat de Barcelona
  • J. A. Subirana
    • Department d'Enginyería Química, ETSEIBUniversitat Politècnica de Catalunya
  • P. Sautière
    • Department de Ciències Fisiològiques Humanes i de la NutricióUniversitat de Barcelona
Article

DOI: 10.1007/BF00160515

Cite this article as:
Daban, M., Martinage, A., Kouach, M. et al. J Mol Evol (1995) 40: 663. doi:10.1007/BF00160515

Abstract

Protamine of the archaeogastropod mollusc Monodonta turbinata has been isolated and characterized. With a mass of 13,476 Da, it is the largest known prolamine. Amino acid sequence of this protamine (106 residues) was established from data provided by automated sequence analysis and mass spectrometry of the protein and of its fragments. The primary structure of the NH2-terminal region exhibits repetitive sequence motifs “Basic-Ser” (mainly R-S) and both central and COOH-terminal regions are composed by arginine clusters. The amino acid sequence of Monodonta turbinata protamine shows structural similarities with other protamines from invertebrates and from birds and mammals.

Key words

ProtamineSperm basic proteinsArchaeogastropodMollusc
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Copyright information

© Springer-Verlag New York Inc 1995