Characterization and N-terminal sequencing of a calcium binding protein from the calcareous concretion organic matrix of the terrestrial crustacean Orchestia cavimana.
We extracted proteins from the organic matrix of calcareous concretions, which represents the calcium storage form in a terrestrial crustacean. Electrophoretic analyses of water-soluble organic-matrix proteinaceous components revealed 11 polypeptides, 6 of which are probably glycosylated. Among the unglycosylated proteins, we characterized a 23 kDa polypeptide, with an isoelectric point of 5.5, which is able to bind calcium. Its N-terminal sequence is rich in acidic amino acids (essentially aspartic acid). All these characteristics suggest its involvement in the calcium precipitation process within the successive layers of the organic matrix.
Luquet
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URA CNRS 674 Développement Communication chimique, Université de Bourgogne, Dijon, France.
Testenière
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Graf
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D000595:Amino Acid Sequence; D000818:Animals; D001224:Aspartic Acid / Q000737:chemistry; D002118:Calcium / Q000378:metabolism*; D002135:Calcium-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D003445:Crustacea / Q000737:chemistry*; D015180:Electrophoresis, Gel, Two-Dimensional; D004591:Electrophoresis, Polyacrylamide Gel; D006020:Glycopeptides / Q000737:chemistry; D008297:Male; D008969:Molecular Sequence Data; D018978:Molting; D010455:Peptides / Q000737:chemistry / Q000378:metabolism
D002135:Calcium-Binding Proteins; D006020:Glycopeptides; D010455:Peptides; D001224:Aspartic Acid; D002118:Calcium