Variability in the preservation of the isotopic composition of collagen from fossil bone

Details Variability in the preservation of the isotopic composition of collagen from fossil bone Variability in the preservation of the isotopic composition of collagen from fossil bone

Apr 1988

adsabs.harvard.edu/cgi-bin/nph-data_query?bibcode=1988gecoa..52..929t&link_type=abstract

Geochimica et Cosmochimica Acta, vol. 52, Issue 4, pp.929-935

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Scientific paper

Collagen from bone was prepared by several methods. For modern and well-preserved bone the 13 C and 15 N of collagen replicas obtained after HCl or EDTA demineralization were similar to those obtained with a gelatinization procedure. However, in more poorly preserved fossil bone the 13 C and 15 N varied among the different protein extracts. The yield of collagen obtained with EDTA demineralization was consistently higher than extraction procedures that used HCl. The 13 C of individual amino acids separated from the collagen of modern and fossil whale bone varied up to 17%., and the 15 N from the same amino acids ranged over 47%. The 13 C and 15 N of most amino acids clustered closely to the average of the HCl insoluble collagen. The 13 C of the major amino acid in collagen, glycine, differed from the average HCl insoluble collagen by approximately 8%. in the fossil whale and 14%. in the modern whale. The 15 N of glycine differed from the average HCl insoluble values by approximately 4%. in the fossil whale and 7%. in the modern whale. Thus, diagenetic changes that alter the ratio of glycine to other amino acids in bone can be expected to perturb the values for carbon and nitrogen isotopes.

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