STRUCTURE AND FUNCTION OF DENTIN MATRIX PROTEINS

这些研究旨在获得一个基本的 了解牙本质基质的结构和功能 proteins. 牙本质基质的详细结构信息 将获得蛋白质及其相互作用。 以这种方式 我们希望在生物化学和分子水平上解释， 组织的功能意义。 为此，我们将 将这些组织分为四个部分， 在形态和生物化学上彼此不同， 可能代表了不同的发展阶段， 基质的矿化。 这些隔间包括 前牙本质蛋白和牙本质蛋白的三个组分（非- 矿化部分，EDTA可提取和不可提取 矿化部分）。 胶原蛋白的定量交叉- 连接分子在牙本质中的分布 将研究胚胎和出生后的牛。 我们将 将这些结果与其他I型糖尿病患者的其他数据进行比较 含有胶原蛋白的组织，以探索其结构- 各种胶原组织之间的功能关系， 在身体中发挥不同的功能。 的信息 这些研究将提供有关立体特异性的数据， 化学交联反应以及有价值的 深入了解胶原蛋白的方位角（角度）取向 纤维中的分子。 我们还将尝试确定结构和分子 磷蛋白相关的交联位点，特别是 假定的结合牙本质的分子间共价交联 在牙本质的各个区室中， 上面引用的。 磷蛋白与 胶原蛋白可能在矿化过程中起重要作用 机制 将通过以下方法分离交联肽： 胰蛋白酶的层析方法 车厢

These studies are directed towards obtaining a basic understanding of the structure and function of dentin matrix proteins. Detailed structural information of dentin matrix proteins and their interactions will be obtained. In this manner we hope to explain on a biochemical and molecular level, this tissue's functional significance. For this purpose, we wil differentiate this tissue into four compartments which are morphologically and biochemically different from each other and may represent the different developmental stages leading to mineralization of the matrix. These compartments include predentin proteins and three fractions of dentin proteins (non- mineralized fraction, EDTA extractable and non-extractable in mineralized fraction). The quantification of the collagen cross- link molecular distribution in these fractions of dentin frmo embryonic and postnatal bovine will be investigated. We shall compare these findings with other data obtained for other Type I collagen containing tissues in order to explore the structure- function relationships among various collagenous tissues that perform different functions in the body. The information from these studies will provide data concerning the stereospecificity of the chemical cross-linking reactions as well as the valuable insights into the azimuthal (angular) orientations of the collagen molecules in the fibrils. We shall also attempt to determine the structure and molecular locus of the phosphoprotein associated cross-links especially the putative intermolecular covalent cross-links that bind the dentin phosphoprotein to collagen, in the various compartments of dentin cited above. Covalent linkage between phosphoprotein and collagen might have an important role for mineralization mechanism. Cross-linked peptides will be isolated by chromatographic methods for tryptic digests of each compartment.