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The soluble calcium-binding protein from muscle of the sandworm, Nereis virens
Gerday, C.; Collin, S.; Gerardin-Otthiers, N. (1981). The soluble calcium-binding protein from muscle of the sandworm, Nereis virens. Journal of Muscle Research and Cell Motility 2(2): 225-238. dx.doi.org/10.1007/BF00711872
In: Journal of Muscle Research and Cell Motility. Springer: Dordrecht. ISSN 0142-4319, more
Peer reviewed article  

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  • Gerday, C., more
  • Collin, S.
  • Gerardin-Otthiers, N.

Abstract
    Fast-acting muscle of the sandworm, Nereis virens, contains one soluble calcium-binding protein having a molecular weight close to 17 000 and occurring in the muscle at a concentration of approximately 0.1mm. The protein binds two Ca2+ at equivalent sites with dissociation constantKd=6.4·10−7m. Its N-terminal amino acid is blocked by an N-acetyl group whereas glycine is the C-terminal residue. The comparison of the tryptic peptide map of this protein with those of the soluble calcium-binding protein from crayfish muscle, bovine brain calmodulin and rabbit skeletal muscle troponin C suggests that all of these proteins are homologous. Sandworm calcium-binding protein therefore belongs to the so-called cytosolic calcium EF-hand family. This protein is presumably the functional counterpart of vertebrate parvalbumin acting as soluble relaxing factor.

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