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钼和钨在体内对胶原蛋白结构的作用机制。

The mechanism of action of molybdenum and tungsten upon collagen structures in vivo.

作者信息

Bíbr B, Deyl Z, Lener J, Kucera J, Simková M

机构信息

Institute of Nuclear Biology and Radiology, Czechoslovak Academy of Sciences, Prague.

出版信息

Physiol Bohemoslov. 1987;36(5):417-24.

PMID:2962207
Abstract

The effect of in vivo administration of molybdenum (as sodium molybdate) and tungsten (as sodium tungstate) was investigated in the skin of laboratory rats. It was proved that the amount of both bound molybdenum and tungsten in collagen is relatively small being 0.05 and 0.06 moles per mole respectively. Besides the fraction of firmly bound molybdenum and tungsten a much higher extractable pool of both these metals was found. It was also demonstrated that in vivo shadowing of collagen is caused by the fraction of loosely bound metals. On the other hand pronounced changes were shown in the mechanical properties of connective tissue after molybdate and tungstate administration. Surprisingly, the change in mechanical properties indicated a lower level of cross-linking after the administration of the investigated metals. It is therefore concluded that bitopical binding of molybdenum and tungsten in the collagen structure is unlikely. It also appears that the biological effect of these metals is due to the competition with copper and the interference with the physiological cross-linking reactions based on the partial blockade of lysyloxidase.

摘要

研究了在实验大鼠皮肤中体内施用钼(以钼酸钠形式)和钨(以钨酸钠形式)的效果。结果证明,胶原蛋白中结合的钼和钨的量相对较少,分别为每摩尔0.05和0.06摩尔。除了牢固结合的钼和钨部分外,还发现这两种金属有更高的可提取池。还证明,胶原蛋白的体内遮蔽是由松散结合的金属部分引起的。另一方面,施用钼酸盐和钨酸盐后,结缔组织的力学性能出现了明显变化。令人惊讶的是,力学性能的变化表明,在所研究的金属施用后,交联水平降低。因此得出结论,钼和钨在胶原蛋白结构中的双位点结合不太可能。还似乎这些金属的生物学效应是由于与铜的竞争以及基于赖氨酰氧化酶部分阻断对生理交联反应的干扰。

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