First proteomic analyses of the dorsal and ventral parts of the Sepia officinalis cuttlebone
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First proteomic investigation on organic matrix compounds of a cuttlefish shell.

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Protein composition of DS and CH parts of S. officinalis shell appear different.

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Shell organic matrices are globally rich in glycoproteins and low pI compounds.

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Most of identified protein compounds contain domains known in biomineralization.

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Our results suggest a transferrin function in the shell DS of S. officinalis.

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