Miles C A, Wardale R J, Birch H L, Bailey A J
Department of Veterinary Medicine, School of Veterinary Science, University of Bristol, Langford, UK.
Equine Vet J. 1994 Jul;26(4):291-6. doi: 10.1111/j.2042-3306.1994.tb04389.x.
Differential scanning calorimetry (DSC) of equine superficial digital flexor tendons revealed the presence of a small exothermic peak at 23 degrees C of unknown origin, and a large endothermic peak at 70 degrees C due to denaturation of cross-linked collagen fibres. In the central degenerated core of damaged tendons the denaturation temperature remained at 70 degrees C but the enthalpy decreased in relation to the extent of degeneration of the tendon. We suggest that this reduction in enthalpy is due to depolymerisation and denaturation of the collagen fibres. This contention is supported by the observed increased activity of the degradative enzyme cathepsin B secreted by the fibroblasts. DSC analysis of cultured porcine tendon fibroblasts revealed a multicomponent endotherm, denaturation beginning at 46 degrees C, a temperature capable of being achieved within the tendon during intensive exercise. DSC clearly has considerable potential in complementing morphological and biochemical studies to determine the aetiology and progress of equine tendon degeneration.
马的浅屈肌腱的差示扫描量热法（DSC）显示，在23℃出现一个来源不明的小放热峰，以及在70℃出现一个由于交联胶原纤维变性导致的大吸热峰。在受损肌腱的中央变性核心区域，变性温度保持在70℃，但焓值随肌腱变性程度而降低。我们认为这种焓值降低是由于胶原纤维的解聚和变性。成纤维细胞分泌的降解酶组织蛋白酶B活性增加支持了这一论点。培养的猪肌腱成纤维细胞的DSC分析显示有一个多组分吸热过程，变性从46℃开始，这一温度在剧烈运动期间的肌腱内能够达到。DSC在补充形态学和生物化学研究以确定马肌腱变性的病因和进展方面显然具有相当大的潜力。
