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α-弹性蛋白凝聚物的钙化:弹性蛋白的一种整体特性。

Calcification of alpha-elastin coacervates: a bulk property of elastin.

作者信息

Urry D W, Hendrix C F, Long M M

出版信息

Calcif Tissue Res. 1976 Aug 3;21(1):57-65. doi: 10.1007/BF02547383.

Abstract

Scanning electron microscopy and electron probe microanalysis studies are reported on thin sections of calcified coacervates of alpha-elastin. It is found that the capacity of elastin coacervates to initiate calcification is a bulk property of the coacervate and not limited to the serum-coacervate interface, that the calcium phosphate deposits act to bind the protein units together and slow the dissolution and spreading of the coacervate as it floats on an airwater interface, and that, within the limits of detectability, there is no involvement of sulfur. As the charged groups of alpha-elastin had been blocked, the initiation of deposition is due to neutral sites in the protein which are tightly bound to the calcium phosphate deposits.

摘要

本文报道了对α-弹性蛋白钙化凝聚层薄片的扫描电子显微镜和电子探针微分析研究。研究发现,弹性蛋白凝聚层引发钙化的能力是凝聚层的整体性质,并非局限于血清-凝聚层界面;磷酸钙沉积物起到将蛋白质单元结合在一起的作用,并减缓凝聚层漂浮在气-水界面时的溶解和扩散;在可检测范围内,没有硫的参与。由于α-弹性蛋白的带电基团已被阻断,沉积的起始是由于蛋白质中的中性位点与磷酸钙沉积物紧密结合。

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