EFFECT OF ALCOHOLS AND NEUTRAL SALT ON THERMAL-STABILITY OF SOLUBLE AND PRECIPITATED ACID-SOLUBLE COLLAGEN
EFFECT OF ALCOHOLS AND NEUTRAL SALT ON THERMAL-STABILITY OF SOLUBLE AND PRECIPITATED ACID-SOLUBLE COLLAGEN
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DOI：
10.1042/bj1310335
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发表时间：
1973-01-01
影响因子：
4.1
通讯作者：
RUSSELL, AE
中科院分区：
文献类型：
--
作者：
RUSSELL, AE
一元和多元醇在KCl的存在下对胶原分子在稀酸溶液中的固有稳定性的影响进行了比较，与相应的溶剂和盐的影响，在盐沉淀的原纤维中的聚集分子的稳定性增加。盐的添加降低了原纤维的溶解度并增加了原纤维的热稳定性，但逐渐降低了溶液中胶原分子的稳定性。与此相反，醇类提高溶解度和降低原纤稳定性，效果增加与溶剂烃链的长度和减少羟基/亚甲基基团的比例。溶解的胶原蛋白由醇的摩尔不稳定性低于原纤维，在低盐浓度下，乙二醇和甘油都是结构稳定剂。电子显微镜的研究表明，盐沉淀的纤维往往采用本机的聚集模式，和定性相似的溶剂的影响，观察到不溶性胶原。在该模型中，静电和非极性相互作用主要是管理过度的胶原纤维的稳定性，而单分子的内在稳定性是极性相互作用和多肽链刚性的函数的实验结果的影响进行了讨论。
The effects of mono- and poly-hydric alcohols in the presence of KCl on the intrinsic stability of collagen molecules in dilute acid solution were compared with corresponding solvent and salt effects on the increased stability of the aggregated molecules in salt-precipitated fibrils. Salt addition decreased solubility and increased the thermal stability of fibrils, but progressively decreased the stability of collagen molecules in solution. In contrast, the alcohols enhanced solubility and decreased fibril stability, the effects increasing with solvent hydrocarbon chain length and with decreasing hydroxyl/methylene-group ratio. Molar destabilization of dissolved collagen by alcohols was lower than for fibrils, and at low salt concentration, both ethylene glycol and glycerol were structural stabilizers. Electron-micrograph studies indicated that salt-precipitated fibrils tended to adopt the native aggregation mode, and qualitatively similar solvent effects were observed in insoluble collagens. Implications of the experimental findings are discussed in terms of a model in which electrostatic and apolar interactions mainly govern the excess of stability in collagen fibrils whereas intrinsic stability of single molecules is a function of polar interactions and polypeptide-chain rigidity.