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Kinetics for birefringence changes in thermally coagulated rat skin collagen

机译:热凝大鼠皮肤胶原蛋白双折射变化的动力学

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Abstract: Thermal fusion or welding of collagen-rich tissues involves the thermal denaturation of collagen which is reflected by changes in birefringence intensity in histologic sections. The weld bond between two severed edges is formed when the apposed ends of the collagen fibrils unravel during heating then re-entwine during the cooling phase. Thermal coagulation of collagen can be described as an end point of a kinetic rate process of thermal damage which is linear with time of exposure and exponential with temperature. The kinetic rate coefficients, A (s$+$MIN@1$/) and E (J/mole), have been experimentally determined for birefringence loss in rat skin collagen heated in vitro - A $EQ 1.606 $MUL 10$+45$/ and E $EQ 3.06 $MUL 10$+5$/. Loss in collagen birefringence is a rare quantitative indicator of thermal damage; in this case, the structural alteration in tissue native-form collagen. The kinetic model coefficients were derived from exposure times between 600 and 6000s over the temperature range 45 to 90$DGR@C. Room temperature control specimens were also analyzed for comparison. !8
机译:摘要:富含胶原蛋白的组织的热融合或焊接涉及胶原蛋白的热变性,这通过组织学切片中双折射强度的变化反映出来。当胶原纤维的对置端在加热过程中解开,然后在冷却阶段重新缠绕时,会在两个切断的边缘之间形成焊接结合。胶原蛋白的热凝结可以描述为热损伤的动力学速率过程的终点,该过程与暴露时间呈线性关系,与温度呈指数关系。动力学速率系数A(s $ + $ MIN @ 1 $ /)和E(J / mole)已通过实验确定了在体外加热的大鼠皮肤胶原蛋白的双折射损失-A $ EQ 1.606 $ MUL 10 $ + 45 $ /和E $ EQ 3.06 $ MUL 10 $ + 5 $ /。胶原蛋白双折射的丧失是热损伤的罕见定量指标。在这种情况下,组织天然胶原蛋白的结构改变。动力学模型系数来自在45至90 $ DGR @ C温度范围内600至6000s的暴露时间。还分析了室温对照样品以进行比较。 !8

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