AMELOGENINS - SEQUENCE HOMOLOGIES IN ENAMEL-MATRIX PROTEINS FROM 3 MAMMALIAN-SPECIES
AMELOGENINS - SEQUENCE HOMOLOGIES IN ENAMEL-MATRIX PROTEINS FROM 3 MAMMALIAN-SPECIES
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DOI：
10.1042/bj2110149
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发表时间：
1983-01-01
影响因子：
4.1
通讯作者：
COTHRAN, WC
中科院分区：
文献类型：
--
作者：
FINCHAM, AG;BELCOURT, AB;COTHRAN, WC
报道了从牛、猪和人类胎儿发育中的牙釉质中分离出的选定釉原蛋白多肽的部分氨基酸序列。所分析的多肽的前28个残基的序列是相同的，无论其来源或大小如何。一种富含酪氨酸的多肽是主要的高分子量釉原蛋白的N -末端片段，尽管在任何其他釉原蛋白结构中未发现大小相似的富含亮氨酸的多肽。这些发现表明细胞外釉质基质的釉原蛋白具有惊人的序列保守程度，并支持在牙釉质矿化过程中初始的30,000道尔顿釉原蛋白分子发生离散断裂这一概念。
Partial amino acid sequences for selected amelogenin polypeptides isolated from the developing enamel of cow, pig and human fetuses are reported. There was an identity of sequence for the initial 28 residues of the polypeptides analyzed, irrespective of their origin or size. A tyrosine-rich polypeptide was the N-terminal fragment of the principal higher MW 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 [dalton] amelogenin molecule during the mineralization of the enamel.