Please use this identifier to cite or link to this item:
|Title:||Purification, characterization, and in vitro mineralization studies of a novel goose eggshell matrix protein, ansocalcin|
|Authors:||Lakshminarayanan, R. |
|Source:||Lakshminarayanan, R., Valiyaveettil, S., Rao, V.S., Kini, R.M. (2003-01-31). Purification, characterization, and in vitro mineralization studies of a novel goose eggshell matrix protein, ansocalcin. Journal of Biological Chemistry 278 (5) : 2928-2936. ScholarBank@NUS Repository. https://doi.org/10.1074/jbc.M201518200|
|Abstract:||Biomineralization is an important process in which hard tissues are generated through mineral deposition, often assisted by biomacromolecules. Eggshells, because of their rapid formation via mineralization, are chosen as a model for understanding the fundamentals of biomineralization. This report discusses purification and characterization of various proteins and peptides from goose eggshell matrix. A novel 15-kDa protein (ansocalcin) was extracted from the eggshell matrix, purified, and identified and its role in mineralization evaluated using in vitro crystal growth experiments. The complete amino acid sequence of ansocalcin showed high homology to ovocleidin-17, a chicken eggshell protein, and to C-type lectins from snake venom. The amino acid sequence of ansocalcin was characterized by the presence of acidic and basic amino acid multiplets. In vitro crystallization experiments showed that ansocalcin induced pits on the rhombohedral faces at lower concentrations (<50 μg/ml). At higher concentrations, the nucleation of calcite crystal aggregates was observed. Molecular weight determinations by size exclusion chromatography and sodium dodecyl sulfate -polyacrylamide gel electrophoresis showed reversible concentration-dependent aggregation of ansocalcin in solution. We propose that such aggregated structures may act as a template for the nucleation of calcite crystal aggregates. Similar aggregation of calcite crystals was also observed when crystallizations were performed in the presence of whole goose eggshell extract. These results show that ansocalcin plays a significant role in goose eggshell calcification.|
|Source Title:||Journal of Biological Chemistry|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Feb 14, 2018
WEB OF SCIENCETM
checked on Jan 23, 2018
checked on Feb 19, 2018
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.