Influence of neutral salts on the hydrothermal stability of acid-soluble collagen
Influence of neutral salts on the hydrothermal stability of acid-soluble collagen
复制标题
DOI：
10.1023/a:1007074314686
复制
发表时间：
2000-02-01
期刊：
影响因子：
--
通讯作者：
Wildermuth, RJ
中科院分区：
文献类型：
--
作者：
Brown, EM;Farrell, HM;Wildermuth, RJ
通过圆二色性（CD）光谱研究了酸溶性胶原蛋白的热稳定性。比较了成人牛真皮胶原蛋白 (BDC)、鼠尾腱胶原蛋白 (RTC) 和小牛皮肤胶原蛋白 (CSC)。尽管氨基酸组成和表观分子量存在一些差异，但所有来源的螺旋和无序胶原结构的 CD 光谱基本上相同。这些胶原蛋白的熔化是一个两阶段过程，其特征是预转变 (T-p)，然后是完全变性 (T-d)。特征温度随胶原蛋白的来源而变化；对于成熟胶原蛋白（BDC、RTC），T-p = 30 摄氏度和 T-d = 36 摄氏度；对于 CSC，T-p = 34 摄氏度和 T-d = 40 摄氏度。低浓度 (0.02-0.2 M) 的中性盐、氯化钠或氯化钾似乎会与胶原蛋白结合，并将这些胶原蛋白的热转变转移到较低的温度。
The thermal stability of acid-soluble collagens was studied by circular dichroism (CD) spectroscopy. Adult bovine dermal collagen (BDC), rat-tail tendon collagen (RTC), and calf skin collagen (CSC) were compared. Despite some variability in amino acid composition and apparent molecular weight, the CD spectra for helical and unordered collagen structures were essentially the same for all the sources. The melting of these collagens occurs as a two-stage process characterized by a pretransition (T-p) followed by complete denaturation (T-d) The characteristic temperatures vary with the source of the collagen; for mature collagens (BDC, RTC) T-p = 30 degrees C and T-d = 36 degrees C, and for CSC T-p = 34 degrees C and T-d = 40 degrees C. Neutral salts, NaCl or KCl, at low concentrations (0.02-0.2 M) appear to bind to the collagens and shift the thermal transitions of these collagens to lower temperatures.