Bio-vaterite formation by glycoproteins from freshwater pearls
- Autores
- Natoli, Antonino; Wiens, Matthias; Schröder, Heinz Christoph; Stifanic, Mauro; Batel, Renato; Soldati, Analía Leticia; Jacob, Dorrit E.; Müller, Werner E.G.
- Año de publicación
- 2010
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- A 48 kDa acidic and putative calcium-binding glycoprotein was isolated from pearls of the freshwater mussel Hyriopsis cumingii. This protein was compared with a related 46 kDa polypeptide, obtained from the nacreous shell of the same species. Separation by two-dimensional gel electrophoresis revealed that the difference in molecular weight is due to the higher extent of glycosylation of the 48 kDa protein existing in pearls. Evidence is presented that the sugar moieties of the protein contribute to crystal growth, starting with the nucleation step. In in vitro precipitation experiments, the 48 kDa glycoprotein of pearls directed the formation of round-shaped vaterite crystals while the 46 kDa glycoprotein of shells promoted formation of small irregular calcite particles. Furthermore, both proteins, 48 kDa/46 kDa, comprised carbonic anhydrase activity that has been implicated in CaCO3 formation. Thus, a function of the isolated glycoproteins in biomineralization is proposed together with the mechanism by which they can stabilize different calcium carbonate polymorphs.
Fil: Natoli, Antonino. Johannes Gutenberg Universitat Mainz; Alemania
Fil: Wiens, Matthias. Johannes Gutenberg Universitat Mainz; Alemania
Fil: Schröder, Heinz Christoph. Johannes Gutenberg Universitat Mainz; Alemania
Fil: Stifanic, Mauro. “Ruder Boskovic” Institute; Croacia
Fil: Batel, Renato. “Ruder Boskovic” Institute; Croacia
Fil: Soldati, Analía Leticia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Patagonia Norte; Argentina. Johannes Gutenberg Universitat Mainz; Alemania
Fil: Jacob, Dorrit E.. Johannes Gutenberg Universitat Mainz; Alemania
Fil: Müller, Werner E.G.. Johannes Gutenberg Universitat Mainz; Alemania - Materia
-
BIOMINERALIZATION
CALCIUM CARBONATE PRECIPITATION
CARBONIC ANHYDRASE
FRESHWATER PEARLS - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
- Repositorio
.jpg)
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/281410
Ver los metadatos del registro completo
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Bio-vaterite formation by glycoproteins from freshwater pearlsNatoli, AntoninoWiens, MatthiasSchröder, Heinz ChristophStifanic, MauroBatel, RenatoSoldati, Analía LeticiaJacob, Dorrit E.Müller, Werner E.G.BIOMINERALIZATIONCALCIUM CARBONATE PRECIPITATIONCARBONIC ANHYDRASEFRESHWATER PEARLShttps://purl.org/becyt/ford/2.5https://purl.org/becyt/ford/2A 48 kDa acidic and putative calcium-binding glycoprotein was isolated from pearls of the freshwater mussel Hyriopsis cumingii. This protein was compared with a related 46 kDa polypeptide, obtained from the nacreous shell of the same species. Separation by two-dimensional gel electrophoresis revealed that the difference in molecular weight is due to the higher extent of glycosylation of the 48 kDa protein existing in pearls. Evidence is presented that the sugar moieties of the protein contribute to crystal growth, starting with the nucleation step. In in vitro precipitation experiments, the 48 kDa glycoprotein of pearls directed the formation of round-shaped vaterite crystals while the 46 kDa glycoprotein of shells promoted formation of small irregular calcite particles. Furthermore, both proteins, 48 kDa/46 kDa, comprised carbonic anhydrase activity that has been implicated in CaCO3 formation. Thus, a function of the isolated glycoproteins in biomineralization is proposed together with the mechanism by which they can stabilize different calcium carbonate polymorphs.Fil: Natoli, Antonino. Johannes Gutenberg Universitat Mainz; AlemaniaFil: Wiens, Matthias. Johannes Gutenberg Universitat Mainz; AlemaniaFil: Schröder, Heinz Christoph. Johannes Gutenberg Universitat Mainz; AlemaniaFil: Stifanic, Mauro. “Ruder Boskovic” Institute; CroaciaFil: Batel, Renato. “Ruder Boskovic” Institute; CroaciaFil: Soldati, Analía Leticia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Patagonia Norte; Argentina. Johannes Gutenberg Universitat Mainz; AlemaniaFil: Jacob, Dorrit E.. Johannes Gutenberg Universitat Mainz; AlemaniaFil: Müller, Werner E.G.. Johannes Gutenberg Universitat Mainz; AlemaniaPergamon-Elsevier Science Ltd2010-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/281410Natoli, Antonino; Wiens, Matthias; Schröder, Heinz Christoph; Stifanic, Mauro; Batel, Renato; et al.; Bio-vaterite formation by glycoproteins from freshwater pearls; Pergamon-Elsevier Science Ltd; Micron; 41; 4; 6-2010; 359-3660968-4328CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/abs/pii/S0968432810000041info:eu-repo/semantics/altIdentifier/doi/10.1016/j.micron.2010.01.002info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2026-06-04T10:51:43Zoai:ri.conicet.gov.ar:11336/281410instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982026-06-04 10:51:43.55CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
| dc.title.none.fl_str_mv |
Bio-vaterite formation by glycoproteins from freshwater pearls |
| title |
Bio-vaterite formation by glycoproteins from freshwater pearls |
| spellingShingle |
Bio-vaterite formation by glycoproteins from freshwater pearls Natoli, Antonino BIOMINERALIZATION CALCIUM CARBONATE PRECIPITATION CARBONIC ANHYDRASE FRESHWATER PEARLS |
| title_short |
Bio-vaterite formation by glycoproteins from freshwater pearls |
| title_full |
Bio-vaterite formation by glycoproteins from freshwater pearls |
| title_fullStr |
Bio-vaterite formation by glycoproteins from freshwater pearls |
| title_full_unstemmed |
Bio-vaterite formation by glycoproteins from freshwater pearls |
| title_sort |
Bio-vaterite formation by glycoproteins from freshwater pearls |
| dc.creator.none.fl_str_mv |
Natoli, Antonino Wiens, Matthias Schröder, Heinz Christoph Stifanic, Mauro Batel, Renato Soldati, Analía Leticia Jacob, Dorrit E. Müller, Werner E.G. |
| author |
Natoli, Antonino |
| author_facet |
Natoli, Antonino Wiens, Matthias Schröder, Heinz Christoph Stifanic, Mauro Batel, Renato Soldati, Analía Leticia Jacob, Dorrit E. Müller, Werner E.G. |
| author_role |
author |
| author2 |
Wiens, Matthias Schröder, Heinz Christoph Stifanic, Mauro Batel, Renato Soldati, Analía Leticia Jacob, Dorrit E. Müller, Werner E.G. |
| author2_role |
author author author author author author author |
| dc.subject.none.fl_str_mv |
BIOMINERALIZATION CALCIUM CARBONATE PRECIPITATION CARBONIC ANHYDRASE FRESHWATER PEARLS |
| topic |
BIOMINERALIZATION CALCIUM CARBONATE PRECIPITATION CARBONIC ANHYDRASE FRESHWATER PEARLS |
| purl_subject.fl_str_mv |
https://purl.org/becyt/ford/2.5 https://purl.org/becyt/ford/2 |
| dc.description.none.fl_txt_mv |
A 48 kDa acidic and putative calcium-binding glycoprotein was isolated from pearls of the freshwater mussel Hyriopsis cumingii. This protein was compared with a related 46 kDa polypeptide, obtained from the nacreous shell of the same species. Separation by two-dimensional gel electrophoresis revealed that the difference in molecular weight is due to the higher extent of glycosylation of the 48 kDa protein existing in pearls. Evidence is presented that the sugar moieties of the protein contribute to crystal growth, starting with the nucleation step. In in vitro precipitation experiments, the 48 kDa glycoprotein of pearls directed the formation of round-shaped vaterite crystals while the 46 kDa glycoprotein of shells promoted formation of small irregular calcite particles. Furthermore, both proteins, 48 kDa/46 kDa, comprised carbonic anhydrase activity that has been implicated in CaCO3 formation. Thus, a function of the isolated glycoproteins in biomineralization is proposed together with the mechanism by which they can stabilize different calcium carbonate polymorphs. Fil: Natoli, Antonino. Johannes Gutenberg Universitat Mainz; Alemania Fil: Wiens, Matthias. Johannes Gutenberg Universitat Mainz; Alemania Fil: Schröder, Heinz Christoph. Johannes Gutenberg Universitat Mainz; Alemania Fil: Stifanic, Mauro. “Ruder Boskovic” Institute; Croacia Fil: Batel, Renato. “Ruder Boskovic” Institute; Croacia Fil: Soldati, Analía Leticia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Patagonia Norte; Argentina. Johannes Gutenberg Universitat Mainz; Alemania Fil: Jacob, Dorrit E.. Johannes Gutenberg Universitat Mainz; Alemania Fil: Müller, Werner E.G.. Johannes Gutenberg Universitat Mainz; Alemania |
| description |
A 48 kDa acidic and putative calcium-binding glycoprotein was isolated from pearls of the freshwater mussel Hyriopsis cumingii. This protein was compared with a related 46 kDa polypeptide, obtained from the nacreous shell of the same species. Separation by two-dimensional gel electrophoresis revealed that the difference in molecular weight is due to the higher extent of glycosylation of the 48 kDa protein existing in pearls. Evidence is presented that the sugar moieties of the protein contribute to crystal growth, starting with the nucleation step. In in vitro precipitation experiments, the 48 kDa glycoprotein of pearls directed the formation of round-shaped vaterite crystals while the 46 kDa glycoprotein of shells promoted formation of small irregular calcite particles. Furthermore, both proteins, 48 kDa/46 kDa, comprised carbonic anhydrase activity that has been implicated in CaCO3 formation. Thus, a function of the isolated glycoproteins in biomineralization is proposed together with the mechanism by which they can stabilize different calcium carbonate polymorphs. |
| publishDate |
2010 |
| dc.date.none.fl_str_mv |
2010-06 |
| dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
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article |
| status_str |
publishedVersion |
| dc.identifier.none.fl_str_mv |
http://hdl.handle.net/11336/281410 Natoli, Antonino; Wiens, Matthias; Schröder, Heinz Christoph; Stifanic, Mauro; Batel, Renato; et al.; Bio-vaterite formation by glycoproteins from freshwater pearls; Pergamon-Elsevier Science Ltd; Micron; 41; 4; 6-2010; 359-366 0968-4328 CONICET Digital CONICET |
| url |
http://hdl.handle.net/11336/281410 |
| identifier_str_mv |
Natoli, Antonino; Wiens, Matthias; Schröder, Heinz Christoph; Stifanic, Mauro; Batel, Renato; et al.; Bio-vaterite formation by glycoproteins from freshwater pearls; Pergamon-Elsevier Science Ltd; Micron; 41; 4; 6-2010; 359-366 0968-4328 CONICET Digital CONICET |
| dc.language.none.fl_str_mv |
eng |
| language |
eng |
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info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/abs/pii/S0968432810000041 info:eu-repo/semantics/altIdentifier/doi/10.1016/j.micron.2010.01.002 |
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info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-nd/2.5/ar/ |
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openAccess |
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https://creativecommons.org/licenses/by-nc-nd/2.5/ar/ |
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application/pdf application/pdf |
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Pergamon-Elsevier Science Ltd |
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Pergamon-Elsevier Science Ltd |
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reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
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Consejo Nacional de Investigaciones Científicas y Técnicas |
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CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
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dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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