Amelogenins. Sequence homologies in enamel-matrix proteins from three mammalian species.
Amelogenins. Sequence homologies in enamel-matrix proteins from three mammalian species.
复制标题
牙釉蛋白。
作者：
A. Fincham;A. Belcourt;J. Termine;W. Butler;W. C. Cothran
报道了从牛、猪和人类胎儿的牙釉质发育中分离的选定牙釉蛋白多肽的部分氨基酸序列。结果发现，所分析的多肽的最初 28 个残基的序列是相同的，无论其来源或大小如何。富含酪氨酸的多肽被证明是主要较高分子量牙釉蛋白的N端片段，尽管在任何其他牙釉蛋白结构中没有鉴定出类似大小的富含亮氨酸的多肽。研究结果表明，细胞外牙釉质基质的牙釉蛋白具有惊人的序列保守性，并支持牙釉质矿化过程中初始 30 000 Da 牙釉蛋白分子离散断裂的概念。
Partial amino acid sequences for selected amelogenin polypeptides isolated from the developing enamel of cow, pig and human foetuses are reported. It was found that there was an identity of sequence for the initial 28 residues of the polypeptides analysed, irrespective of their origin or size. A tyrosine-rich polypeptide was shown to be the N-terminal fragment of the principal higher-molecular-weight amelogenins, although a leucine-rich polypeptide of similar size was not identified in any other amelogenin structure. The findings demonstrate a striking degree of sequence conservation for the amelogenin proteins of the extracellular enamel matrix and support the concept of a discrete fragmentation of an initial 30 000 Da amelogenin molecule during the mineralization of the enamel.