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Biochemical analyses of fossil enamel and dentin

Published online by Cambridge University Press:  08 April 2016

Melvin J. Glimcher ,
Lola Cohen-Solal ,
Dora Kossiva  and
Armand de Ricqles
Melvin J. Glimcher
Affiliation:
Department of Orthopaedic Surgery, Harvard Medical School, Children's Hospital, 300 Longwood Avenue, Boston, Massachusetts 02115
Lola Cohen-Solal
Affiliation:
INSERM, Unite de Recherches de Genetique Medicale, Hôpital des Enfants Malades, 149, rue de Sèvres, 75730 Paris Cedex 15, France
Dora Kossiva
Affiliation:
Department of Orthopaedic Surgery, Harvard Medical School, Children's Hospital, 300 Longwood Avenue, Boston, Massachusetts 02115
Armand de Ricqles
Affiliation:
Laboratoire d'Anatomie Comparée, Universite Paris VII, Equipe de recherche “formations squelethiques,” 75251 Paris Cedex 05, France
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Abstract

Amino acid analyses of undecalcified samples of fossil crocodile and rhinoceros enamel and dentin from mature teeth revealed that the total protein content of these mineralized fossil tissues varied from ~0.01–0.007% by weight. Except in one instance, amino acid analyses of the enamel proteins revealed them to be free of collagen and to have an amino acid composition similar to the proteins obtained from the enamel of mature modern vertebrates. Molecular sieving of the acid soluble enamel proteins demonstrated that the components consisted principally of small peptides and free amino acids, as in the enamel of modern vertebrates.

Based on the presence of hydroxyproline (hyp) and hydroxylysine (hyl), collagen was detected in undecalcified mature dentin of fossil rhinoceros, but not in undecalcified crocodile dentin. It was only by sequential extraction procedures that the presence of collagen in the dentin of fossil crocodile was established, emphasizing the utility and importance of analyzing the soluble components in specific extracts of the fossil. Based on these data and the concentrations of hyp and hyl in the material solubilized by the various solvents, the dentin of fossil rhinoceros contained considerably more collagen per weight and as a percentage of the total protein in the dentin than did the dentin of fossil crocodile.

As with modern dentin, EDTA and dilute acid solubilize the noncollagenous proteins and peptides found in fossil enamel and dentin, some of which contain O-phosphoserine [Ser(P)], an amino acid unique to mineralized connective tissues. Similar to recent reported findings from fossil bone, less of the original content of the noncollagenous proteins, including those phosphorylated, is degraded and removed from the enamel and dentin during fossilization than the percentage of dentinal collagen and the nonphosphorylated domains of the enamel proteins which are removed. This selective resistance to degradation and removal of the noncollagenous proteins, including phosphoproteins, may reflect the strong interaction of these proteins with the mineral phase of fossilized tissues. The amount and close packing of the inorganic crystals may also inhibit the interaction of the proteins in the interior of the enamel and dentin with the geochemical environment.

Type
Articles
Information
Paleobiology , Volume 16 , Issue 2 , Spring 1990 , pp. 219 - 232
Copyright
Copyright © The Paleontological Society 

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