GROSS J
Science. 1964 Feb 28;143(3609):960-1. doi: 10.1126/science.143.3609.960.
Thermal denaturation temperature of newly reconstituted collagen fibrils from rat tail tendons is 52 degrees C compared with 42 degrees C for neutral solutions. This suggests that the increase in concentration of collagen within the fibril increases the stability of the individual molecules. The absence of firm intermolecular bonds in these fibrils rules out crosslinking as an explanation for increased stability. "Aging" at 37 degrees C up to 1 year raises the shrinkage temperature of reconstituted fibrous gels by 4 degrees to 6 degrees C and greatly increases resistance to dissolution at high temperature. The newly formed fibrils dissolve without shrinking, whereas older gels exhibit shrinkage before dissolution. Since nearly all extractable collagen is in the form of fibrillar aggregates in tissue, it is unlikely that thermal denaturation occurs at body temperature; therefore it could not be involved as a necessary stage in collagen resorption.
大鼠尾腱新重构胶原纤维的热变性温度为52摄氏度，而中性溶液中的为42摄氏度。这表明纤维内胶原浓度的增加提高了单个分子的稳定性。这些纤维中不存在牢固的分子间键，排除了交联是稳定性增加的原因。在37摄氏度下“老化”长达1年，可使重构纤维凝胶的收缩温度提高4至6摄氏度，并大大增加高温下的抗溶解能力。新形成的纤维溶解时不收缩，而较老的凝胶在溶解前会收缩。由于组织中几乎所有可提取的胶原都是纤维状聚集体形式，因此热变性不太可能在体温时发生；所以它不可能是胶原吸收过程中的一个必要阶段。
