The renaturation of soluble collagen. Products formed at different temperatures.
The renaturation of soluble collagen. Products formed at different temperatures.
复制标题
可溶性胶原蛋白的复性。
DOI：
10.1021/bi00872a035
复制
发表时间：
1966
期刊：
影响因子：
2.9
通讯作者：
J. Engel
中科院分区：
文献类型：
--
作者：
G. Beier;J. Engel
摘要：在pH 3.7的0.25 m柠檬酸缓冲液中，在4-30℃的温度范围内等温研究了不同浓度酸溶性小牛皮胶原的螺旋-螺旋转变。随着时间的推移，负旋光性和粘度的恢复以及原生分子的重新形成也随之发生。通过超离心分析、胃蛋白酶攻击和熔融行为对不同温度下形成的产物进行了研究。研究发现，在等温条件下，天然分子确实发生了再形成。然而，在低还原温度下，这种反应被其他稳定形式的竞争性快速形成所抑制。它们是高分子量的聚集体，含有抗胃蛋白酶的螺旋区域，由胃蛋白酶可消化的非螺旋链部分连接。它们的形成是在这些条件下光学旋转快速恢复的原因。螺旋状区域似乎具有胶原蛋白样的三股结构，但它们的
Gundolf Beier and Jurgen Engel abstract: The coil-helix transition of acid-soluble calfskin collagen dissolved in 0.25 m citrate buffer, pH 3.7, was studied isothermally over a temperature range of 4-30 at severalconcentrations. Recovery of negative optical rotation and viscosityand the re-formation of nativemolecules have been followedwith time. The products formed at different temperatures have been examined by ultracentrifuge analysis, pepsin attack, and by their melting behavior. It was found that a re-formation of native molecules does occur under isothermal conditions. At low renaturation temperatures, however, this reaction is suppressed by a compet-ing rapid formation of other stabilization forms. These are high molecular weight aggregates containing pepsinresistant, helical regions connected by pepsin-digestible, nonhelical chain parts. Theirformation is re-sponsible for the high and fast recovery of optical rota-tion underthose conditions. The helical regions seem to assume a collagen-like three-strand structure, but their