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The amelogenins are the most abundant proteins in developing tooth enamel. Previous analyses have demonstrated that transcriptionally active genes encoding the proteins are located on both the bovine X and the bovine Y chromosomes. We report here the cloning and sequence analysis of the Y-chromosomal gene and corresponding cDNA. The Y-specific mRNA encodes a translation product in which a 21 amino acid domain has been deleted, relative to the X-specific amelogenin, resulting in loss of a structure tentatively described as a beta-spiral. There are also 13 single amino acid differences compared to the X-specific amelogenin. In addition, we have cloned and sequenced an X-chromosomal alternatively spliced amelogenin cDNA that encodes a 43 amino acid amelogenin primary translation product. Hydrophobicity analysis indicates that all analyzed amelogenin proteins have a mean hydrophilic character and the two peptides translated from alternatively spliced messages have significant increases in percentage of hydrophobic amino acids.
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Gibson et al. (1992) studied this question.
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