The protein of pigmented Polynesian dental enamel.
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 non-amelogenins. 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 non-amelogenin. This contrasts with hypomaturation amelogenesis imperfecta in which the protein has the amino acid profile of amelogenin.
Smillie
A C
AC
Faculty of Dentistry, University of Otago, Dunedin, New Zealand.
Rodda
J C
JC
Young
D
D
D000293:Adolescent; D000328:Adult; D000567:Amelogenesis Imperfecta / Q000473:pathology*; D053523:Amelogenin; D000596:Amino Acids / Q000032:analysis; D002648:Child; D003746:Dental Enamel Proteins / Q000032:analysis / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D005006:Ethnicity; D005260:Female; D006801:Humans; D008297:Male; D008970:Molecular Weight; D009520:New Zealand; D011114:Polynesia
D053523:Amelogenin; D000596:Amino Acids; D003746:Dental Enamel Proteins