Comparison of dynamic denaturation temperature of collagen with its static denaturation temperature and the configuration characteristics in collagen denaturation processes
作者： Yang Li , Yanwen Li , Zongliang Du , Guoying Li
DOI: 10.1016/J.TCA.2008.01.006
关键词: Viscometer 、 Differential scanning calorimetry 、 Apparent viscosity 、 Intrinsic viscosity 、 Chemistry 、 Denaturation (biochemistry) 、 Shear rate 、 Circular dichroism 、 Analytical chemistry 、 Viscoelasticity
摘要: Abstract Exposing collagen to a sinusoidally fluctuating strain, dynamic denaturation temperature (Tdd) of was obtained by measuring its viscoelasticity changes depended on using rheometer, and it compared with static (Tsd), which determined both differential scanning calorimeter (DSC) specific viscosity only an Ubbelohde viscosimeter. The results showed that Tdd 31.1 °C about 4 °C lower than Tsd. apparent caused increasing shear rate were reversible when sheared at 28.5 °C, but they irreversible 33 °C. sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE), circular dichroism (CD) fibril formation experiments 28.5 °C could keep triple helical structure the helix 33 °C transformed random coils, indicating heat-denatured. However heated did not denature kept native configuration. revealed shearing induce decrease collagen.
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