ポスター発表
- 第2日 5月16日（火） P会場（ホワイエ，会議室1004-1007）
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2P-13 PDF
質量分析と電気泳動を用いた化石残存タンパク質の解析
Paleoproteomics, the study of protein in fossils, has rapidly developed since the development of mass spectrometry and soft ionization. However, the possibility of contamination has been a persistent concern, necessitating the development of multifaceted methods for Paleoproteomic analysis. In this study, we investigated the effectiveness of electrophoresis and mass spectrometry, histological analysis, and colorimetric analysis as protein detection methods for fossil samples. We sampled Pleistocene elephantid rib, ulna and incisor specimens recovered in the Bisan-Seto area. SDS-PAGE, colorimetric assays, and HE staining of decalcified samples detected proteins in bone samples, while no detectable proteins in incisor samples. We performed MALDI-TOF-TOF MS analysis on the protein bands obtained from the rib sample. The spectra were analyzed using the Mascot search engine as well as de novo sequencing and the BLAST search. Both analyses identified the type I collagen of an extinct elephant species. These results indicate that we successfully recovered endogenous fossil proteins from the bone samples. The different protein recovery rates between bone and incisor samples could be explained by the difference in the microstructure. These results demonstrate that protein extraction from bones rather than teeth improve protein extraction results, providing better result in mass spectrometry.