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Journal Article

Purification of ovocalyxin-32, a novel chicken eggshell matrix protein

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http://pubman.mpdl.mpg.de/cone/persons/resource/persons78355

Mann,  K.
Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society;
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

Hincke, M. T., Gautron, J., Mann, K., Panheleux, M., McKee, M. A., Bain, M., et al. (2003). Purification of ovocalyxin-32, a novel chicken eggshell matrix protein. Connective Tissue Research, 44(Suppl. 1), 16-19.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-6D00-7
Abstract
The eggshell is a highly ordered structure resulting from the deposition of calcium carbonate and an organic matrix from the acellular uterine fluid. Characterization of the individual matrix components is necessary to determine their influence upon calcite crystal shape, size, and orientation during eggshell calcification. We have purified and sequenced a novel 32-kDa protein, ovocalyxin-32 (OCX-32), which is present at high levels in the uterine fluid during the terminal phase of eggshell formation, and is localized predominantly in the outer eggshell. Database searches identified expressed sequence tags (ESTs) whose alignment yielded the complete cDNA. OCX-32 protein possesses limited identity (32%) to two unrelated proteins: latexin, a carboxypeptidase inhibitor expressed in rat cerebral cortex and mast cells, and to a skin protein that is encoded by a retinoic acid receptor-responsive gene, TIG1. The timing of OCX-32 secretion into the uterine fluid suggests that it may play a role in the termination of mineral deposition.