Abstract
This enamel contained 1.4–3.7% protein, calculated from amino acid residues, in which glutamic acid and leucine were the most generally abundant and lysine was the most abundant basic amino acid. The amino acid profiles of both French Polynesian and Maori pigmented enamel protein were similar and closely resembled that of tuft protein and certain nondashamelogenins. Sodium dodecyl sulphate-polyacrylamide gel electrophoresis of extracts of pigmented enamel showed an absence of amelogenin protein and the presence of two principal proteins at M r 55,000–66,000, indicating that the protein of pigmented Polynesian enamel was nondashamelogenin. This contrasts with hypomaturation amelogenesis imperfecta in which the protein has the amino acid profile of amelogenin.
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