دورية أكاديمية
Proteomic identification of novel proteins from the calcifying shell matrix of the Manila clam Venerupis philippinarum.
| العنوان: | Proteomic identification of novel proteins from the calcifying shell matrix of the Manila clam Venerupis philippinarum. |
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| المؤلفون: | Marie, Benjamin, Trinkler, Nolwenn, Zanella-Cléon, Isabelle, Guichard, Nathalie, Becchi, Michel, Paillard, Christine, Marin, Frédéric |
| المساهمون: | Biogéosciences UMR 6282 (BGS), Université de Bourgogne (UB)-Centre National de la Recherche Scientifique (CNRS), Laboratoire des Sciences de l'Environnement Marin (LEMAR) (LEMAR), Institut de Recherche pour le Développement (IRD)-Institut Français de Recherche pour l'Exploitation de la Mer (IFREMER)-Université de Brest (UBO)-Institut Universitaire Européen de la Mer (IUEM), Institut de Recherche pour le Développement (IRD)-Institut national des sciences de l'Univers (INSU - CNRS)-Université de Brest (UBO)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD)-Institut national des sciences de l'Univers (INSU - CNRS)-Université de Brest (UBO)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Institut de biologie et chimie des protéines Lyon (IBCP), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), Supports from the "Conseil Régional de Bourgogne" (Dijon, France). |
| المصدر: | ISSN: 1436-2228. |
| بيانات النشر: | HAL CCSD Springer Verlag |
| سنة النشر: | 2011 |
| المجموعة: | HAL Lyon 1 (University Claude Bernard Lyon 1) |
| مصطلحات موضوعية: | Biomineralization, Calcium carbonate, Proteomics, Mollusc shell, Organic matrix, Calcium-binding protein, Serine protease inhibitor, [SDV.IB.BIO]Life Sciences [q-bio]/Bioengineering/Biomaterials |
| الوصف: | 8 pages ; International audience ; The shell of the Manila clam Venerupis philippinarum is composed of more than 99% calcium carbonate and of a small amount of organic matrix (around 0.2%). In this study, we developed one of the first proteomic approaches applied to mollusc shell in order to characterise the matrix proteins that are believed to be essential for the formation of the biomineral. The insoluble organic matrix, purified after demineralisation of the shell powder with cold acetic acid (5%), was digested with trypsin enzyme and then separated on nano-LC prior to nanospray/quadrupole time-of-flight analysis. MS/MS spectra were searched against the above 11,000 EST sequences available on the NCBI public database for Venerupis. Using this approach, we were able to identify partial or full-length sequence transcripts that encode for shell matrix proteins. These include three novel shell proteins whose sequences do not present any homologous proteins or already described domains, two putative protease inhibitor proteins containing Kazal-type domains, and a putative Ca(2+)-binding protein containing two EF-hand domains. Biomineral formation and evolutionary implications are discussed. |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| العلاقة: | info:eu-repo/semantics/altIdentifier/pmid/21221694; hal-00614936; https://hal.science/hal-00614936Test; PUBMED: 21221694 |
| DOI: | 10.1007/s10126-010-9357-0 |
| الإتاحة: | https://doi.org/10.1007/s10126-010-9357-0Test https://hal.science/hal-00614936Test |
| رقم الانضمام: | edsbas.936B6997 |
| قاعدة البيانات: | BASE |
| DOI: | 10.1007/s10126-010-9357-0 |
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