Abstract
The extracellular protein matrix of developing enamel includes a major class of proteins, the amelogenins, which are believed to be concerned in regulating enamel biomineralization. Previous studies have shown the amelogenins of the extracellular matrix to be a complex of proline-rich hydrophobic proteins which, it is suggested, arise through posttranslational and postsecretory processing of a primary ameloblast gene product. More recently, it has been shown that the human amelogenin gene is located on both the X and Y chromosomes raising the possibility that polymorphism at the level of the gene may also contribute to the observed complexity of these enamel matrix proteins. To investigate such possible amelogenin polymorphism in developing human dental enamel, individual fractionated by size-exclusion and reversed-phase high pressure liquid chromatography (HPLC). Two tyrosine-rich amelogenin polypeptides (TRAPs) of approximately 5 kDa in size were isolated from an individual human dentition and characterized by automated gas-phase sequencing. These polypeptides were found to be of 42 (TRAP-2) and 44 (TRAP-1) amino acid residues in length; TRAP-2 lacked a carboxy-terminal -Gly-Trp sequence as has previously been described for a...Continue Reading
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