Tsereteli G I, Belopol'skaia T V, Anisimov V N
Biofizika. 1996 May-Jun;41(3):658-64.
By means of differential scanning calorimetry we have studied the influence of structural changes induced by the biological aging on the processes of thermal denaturation of collagen tissue (rat tail tendon, age from 14 days to 24 months). We have found that some parameters of the thermal denaturation process, namely, the denaturation temperature Td and the denaturation heat Qd are sensitive to the biological age of the tissue. Both Td and Qd are increasing with the age. However, this increase takes place only on early stages of aging. When the denaturation heat Qd of the tissue is normalized on the content of collagen in it, one obtains the independent on the age value of 75 J/g. So the increase of Qd with aging reflects the increase of the collagen content in tissue. We have found that the half-widths of the denaturation curves delta T 1/2, as well as the heat capacity increment at denaturation delta Cp do not depend on the tissue age. Both for fibrills of collagen and for its solution the measured value of delta Cp is equal 0.42 +/- 0.004 J/g degrees C which differs considerably from the earlier published data.
通过差示扫描量热法，我们研究了生物衰老引起的结构变化对胶原组织（大鼠尾腱，年龄从14天到24个月）热变性过程的影响。我们发现，热变性过程的一些参数，即变性温度Td和变性热Qd对组织的生物年龄敏感。Td和Qd都随年龄增加。然而，这种增加仅发生在衰老的早期阶段。当将组织的变性热Qd按其中胶原蛋白的含量进行归一化时，得到的与年龄无关的值为75 J/g。因此，Qd随衰老的增加反映了组织中胶原蛋白含量的增加。我们发现，变性曲线的半高宽δT 1/2以及变性时的热容增量δCp与组织年龄无关。对于胶原纤维及其溶液，测得的δCp值均为0.42±0.004 J/g·℃，这与早期发表的数据有很大差异。
