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矿化与脱矿牙本质的热稳定性:差示扫描量热法研究

Thermal stability of mineralized and demineralized dentin: a differential scanning calorimetric study.

作者信息

Sakae T, Mishima H, Kozawa Y, LeGeros R Z

机构信息

Department of Anatomy, Nihon University School of Dentistry at Matsudo, Chiba, Japan.

出版信息

Connect Tissue Res. 1995;33(1-3):193-6. doi: 10.3109/03008209509017001.

Abstract

The purpose of this study was to determine the difference, if any, in the thermal stability of collagen in mineralized and demineralized dentine compared to that in unmineralized tissues, using differential scanning calorimetry, DSC. Human tooth dentin blocks, about 1 x 1 x 2 mm in size, were used in this study. Some dentin blocks were demineralized using a Plank Rychlo solution; others, using EDTA solution. The mineralized dentin showed an exothermic peak at about 310 degrees C and the combustion of organic materials was completed at about 450 degrees C. For the demineralized dentin, the combustion was completed at higher temperature range and showed a strong exothermic peak at about 470 degrees C. An exotherm at the temperature between 450 degrees C and 470 degrees C was also observed in DSC pattern of native type I collagen from calf skin and rat tail tendon. DSC pattern of rat tail collagen showed a close similarity to that of the demineralized dentin. Statistically, the same heat flow value was obtained both from the mineralized dentin and the demineralized dentin and from the native type I collagen. These findings indicated that the thermal stability of collagen in dentin is lower than collagen in uncalcified connective tissue. It is suggested that in calcified collagen, the apatite crystallites may have intruded into spaces of the crosslinks of intra- and inter-fibrils, and in so doing, destroyed the crosslinks.

摘要

本研究的目的是使用差示扫描量热法(DSC)来确定矿化和脱矿牙本质中胶原蛋白的热稳定性与未矿化组织中胶原蛋白的热稳定性之间是否存在差异(若有差异)。本研究使用了尺寸约为1×1×2毫米的人牙本质块。一些牙本质块用普兰克·雷克洛溶液脱矿;另一些用乙二胺四乙酸(EDTA)溶液脱矿。矿化牙本质在约310℃处显示一个放热峰,有机材料的燃烧在约450℃时完成。对于脱矿牙本质,燃烧在更高温度范围内完成,并在约470℃处显示一个强烈的放热峰。在来自小牛皮肤和大鼠尾腱的天然I型胶原蛋白的DSC图谱中也观察到在450℃至470℃之间的温度处有一个放热峰。大鼠尾胶原蛋白的DSC图谱与脱矿牙本质的DSC图谱显示出密切的相似性。从统计学角度来看,矿化牙本质、脱矿牙本质以及天然I型胶原蛋白获得的热流值相同。这些发现表明,牙本质中胶原蛋白的热稳定性低于未钙化结缔组织中的胶原蛋白。有人提出,在钙化胶原蛋白中,磷灰石微晶可能侵入了原纤维内和原纤维间交联的空间,从而破坏了交联。

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