BIOMINERALIZATION IN THE PRESENCE OF CALCIUM-BINDING PHOSPHOPROTEIN PARTICLES
BIOMINERALIZATION IN THE PRESENCE OF CALCIUM-BINDING PHOSPHOPROTEIN PARTICLES
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DOI：
10.1002/jez.1402390208
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发表时间：
1986-08-01
影响因子：
--
通讯作者：
MARSH, ME
中科院分区：
文献类型：
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作者：
MARSH, ME
河口蛤Rangia cuneata的最内层壳层是一个动态结构，其组成是可变的。在某些种群中，片层是缺乏结晶矿物的富含磷蛋白的结构，而在另一些种群中，片层是富含葡糖胺的结构，通常含有重晶石（BaSO 4）夹杂物。矿物沉积是人为刺激Rangia含有富含葡糖胺lamabrium划伤内壳表面。刺激后，lameprotein转化为富含磷蛋白的结构，其中文石（CaCO3）沉积。该矿物生长在球晶和哑铃形簇特征的文石沉淀从严格的无机溶液。这项研究表明，磷蛋白颗粒积累在最内层壳层在刺激生物矿化，但既不抑制矿物沉积，也不影响晶体的习惯。由于磷蛋白颗粒是高容量的钙结合蛋白，它们可能是用于壳矿化的钙离子的来源和运输工具。
The innermost shell lamella, which coats the inner surface of the shells in the estuarine clam Rangia cuneata, is a dynamic structure with a variable composition. In some populations the lamella is a phosphoprotein-rich structure devoid of crystalline mineral, and in others it is a glucosamine-rich structure often containing barite (BaSO4) inclusions. Mineral depositions was artificially stimulated in Rangia containing glucosamine-rich lamellae by scratching the inner shell surface. After stimulation, the lamellae were transformed into phosphoprotein-rich structures in which aragonite (CaCO3) was deposited. The mineral grew in spherulitic and dumbbell-shaped clusters characteristic of aragonite precipitated from strictly inorganic solutions. This study demonstrates that phosphoprotein particles accumulate in the innermost shell lamella during stimulated biomineralization but neither inhibit mineral deposition nor influence the crystal habits. Since phosphoprotein particles are high capacity calcium-binding proteins, they may be the source and transport vehicle for the calcium ions utilized in shell mineralization.