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Extraction of osteocalcin from fossil bones and teeth
M M Ulrich1, W R Perizonius, C F Spoor
1Department of Biochemistry, University of Limburg, Maastricht, The Netherlands.
Biochemical and Biophysical Research Communications
|December 16, 1987
Summary
Osteocalcin, a bone protein, was found intact in ancient animal fossils up to 13 million years old. This discovery may allow for amino acid sequencing, advancing the study of extinct species
Area of Science:
- Paleoproteomics
- Biochemistry
- Evolutionary Biology
Background:
- Osteocalcin (bone Gla-protein) is a key non-collagenous bone matrix protein.
- Its stability and presence in fossilized remains are crucial for understanding ancient biology.
Purpose of the Study:
- To detect and characterize osteocalcin in fossilized bovid bones and rodent teeth.
- To assess the potential for amino acid sequencing of ancient osteocalcin for phylogenetic analysis.
Main Methods:
- Detection of osteocalcin in fossil samples using immunological and biochemical techniques.
- Analysis of intact Gla-residues and antigenic activity.
- High-Performance Liquid Chromatography (HPLC) with ion exchange and size exclusion columns to compare with modern osteocalcin.
Main Results:
- Osteocalcin was successfully detected in fossil bovid bones (12,000 to 13 million years old) and rodent teeth (30 million years old).
- Both antigenic activity and protein-bound Gla-residues were preserved in the ancient osteocalcin.
- The fossil osteocalcin was indistinguishable from recent bovine osteocalcin via HPLC analysis.
Conclusions:
- Osteocalcin is remarkably stable and detectable in ancient fossilized materials over millions of years.
- The preservation of osteocalcin's structure offers a potential new avenue for determining amino acid sequences from fossils.
- This could revolutionize phylogenetic studies of extinct taxa by providing molecular data from ancient specimens.
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