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首页> 外文期刊>Spectrochimica acta, Part A. Molecular and biomolecular spectroscopy >Collagen absorption bands in heated and rehydrated dentine
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Collagen absorption bands in heated and rehydrated dentine

机译：加热和复水的牙本质中的胶原吸收带

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The objective of this work is identifying changes in the collagen bands in heated and rehydrated dentine. We use bovine dentine slices that were heated in oven between 100 and 300 degrees C. The sample hydration was conducted in sodium chloride solution at 0.9 wt.%; the spectra were acquired by a Fourier transform infrared spectrometer in the spectral range of 4000-400 cm(-1). Our results show a temperature range (T <= 175 degrees C where the dentinal collagen can be partially denatured and reverted to initial conformation; a second region (175 degrees C< T< 225 degrees C) where this process occurs partially and a third region (T> 225 degrees C) where the collagen is denatured and no reversion is observed after rehydration. This work identifies an important characteristic that dentinal collagen can assume when the tissue is heated and rehydrated; these results indicate the denaturation temperature of dentinal collagen to be near 175-200 degrees C. (c) 2005 Elsevier B.V. All rights reserved.
机译：这项工作的目的是确定加热和再水合的牙本质中胶原蛋白带的变化。我们使用在烤箱中加热100至300摄氏度的牛牙质切片。样品的水合在0.9％的氯化钠溶液中进行;光谱是通过傅立叶变换红外光谱仪在4000-400 cm（-1）的光谱范围内获得的。我们的结果显示，温度范围（T <= 175摄氏度，其中牙本质胶原可以部分变性并恢复为初始构象）;第二个区域（175摄氏度，T <225摄氏度），该过程部分发生;第三区域（T> 225°C）胶原蛋白变性，补液后未见逆转，这项工作确定了牙本质胶原蛋白在加热和补液后可以承担的重要特征;这些结果表明牙本质胶原蛋白的变性温度为接近175-200摄氏度。（c）2005 Elsevier BV保留所有权利。

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