RECONSTITUTION OF ELASTIN FROM A SOLUBLE PROTEIN DERIVED FROM LIGAMENTUM-NUCHAE
RECONSTITUTION OF ELASTIN FROM A SOLUBLE PROTEIN DERIVED FROM LIGAMENTUM-NUCHAE
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DOI：
10.1042/bj0690539
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发表时间：
1958-01-01
影响因子：
4.1
通讯作者：
WOOD, GC
中科院分区：
文献类型：
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作者：
WOOD, GC
从牛项韧带制备的可溶性弹性蛋白的高分子量[α]级分（Adair等人，1951）在某些条件下长时间加热水溶液时变得不溶。热沉淀弹性蛋白具有纯化弹性蛋白的许多物理性质，并且可以得出结论，蛋白质分子在2种材料中具有基本相同的构型。热沉淀（重构）弹性蛋白和纯化的弹性蛋白之间的差异可能是由于后者在转化为可溶性弹性蛋白时发生降解。弹性蛋白的沉淀似乎由两个过程组成，即可能涉及构型变化并导致凝聚的快速过程和可能由于蛋白质分子聚集而导致的缓慢过程。本文还讨论了弹性蛋白的结构及其纤维化的结果。
The high-molecular-weight [alpha]-fraction of soluble elastin prepared from ox ligamentum nuchae (Adair et al. 1951) becomes insoluble on prolonged heating of aqueous solutions under certain conditions. Heat-precipitated elastin has many of the physical properties of purified elastin and it is concluded that the protein molecules have essentially the same configuration in the 2 materials. Differences between heat-precipitated (reconstituted) elastin and purified elastin may be attributed to degradation of the latter when it is converted into soluble elastin. The precipitation of elastin appears to consist of two processes, namely a rapid one which may involve configurational changes and results in coacervation and a slow one which is probably due to aggregation of the protein molecules. The bearing of the results of the structure of elastin and its fibrogenesis is discussed.