Epimerization of COOH-terminal isoleucine in fossil dipeptides

Details Epimerization of COOH-terminal isoleucine in fossil dipeptides Epimerization of COOH-terminal isoleucine in fossil dipeptides

May 1983

adsabs.harvard.edu/cgi-bin/nph-data_query?bibcode=1983gecoa..47..963k&link_type=abstract

Geochimica et Cosmochimica Acta, vol. 47, Issue 5, pp.963-966

Physics

3

Scientific paper

Using procedures employed for protein sequencing to remove NH 2 -terminal amino acids, the degree of epimerization of COOH-terminal isoleucine in dipeptides from fossil mollusc shells has been measured directly. The results show that isoleucine in this position is highly epimerized in fossil dipeptides and that the COOH-terminal isoleucine is more highly epimerized than the free amino acid. Hydrolysis of the highly epimerized terminal isoleucine leads to the high alloisoleucine/isoleucine values found in the free amino acid fraction. The results also provide evidence for the formation of diketopiperazines in fossils as a mechanism to account for the high degree of epimerization of COOH-terminal isoleucine.

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