Identification of Animal Species of Collagen Used as Glues in Archaeological Materials Utilizing MALDI Mass Spectrometry
Project/Area Number |
22820042
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Research Category |
Grant-in-Aid for Research Activity Start-up
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Allocation Type | Single-year Grants |
Research Field |
Archaeology
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Research Institution | Nara Women's University |
Principal Investigator |
KAWAHARA Kazuki 奈良女子大学, 古代学学術研究センター, 特任助教 (60585058)
|
Project Period (FY) |
2010 – 2011
|
Project Status |
Completed (Fiscal Year 2011)
|
Budget Amount *help |
¥3,016,000 (Direct Cost: ¥2,320,000、Indirect Cost: ¥696,000)
Fiscal Year 2011: ¥1,443,000 (Direct Cost: ¥1,110,000、Indirect Cost: ¥333,000)
Fiscal Year 2010: ¥1,573,000 (Direct Cost: ¥1,210,000、Indirect Cost: ¥363,000)
|
Keywords | 考古学 / 膠 / コラーゲン / プロテオミクス / 質量分析 |
Research Abstract |
Collagen, the most abundant protein in animals, has often been found as animal glue in a wide variety of archaeological materials. In this research project, we propose a methodology for unambiguously identifying animal glues in archeological materials, based on the matrix-assisted laser desorption/ionization time-of-flight(MALDI-TOF) mass spectrometry. According to ancient records, the animal glue can be prepared from a variety of animals such as cow, deer, fish, donkey, and rabbit. Despite very few substitutions of amino acids found in peptide peaks in the MALDI spectra of tryptic digest of such animal glues, we could distinguish among different animals including cow, deer, fish, and rabbit. Employing these peaks as markers, we identified type I collagen & possibly from cow for the glue of ink sticks manufactured about 270 and 1300 years ago in Nara, Japan.
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Report
(3 results)
Research Products
(23 results)
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[Journal Article] Polymorphism of Collagen Triple Helix Revealed by (19)F NMR of Mode 1 Peptide [Pro-4(R)-Hydroxyprolyl-Gly](3)-[Pro-4(R)-Fluoroprolyl-Gly]-[Pro-4(R)-Hydroxyprolyl-Gly](3)2012
Author(s)
Kawahara K, Nemoto N, Motooka D, Nishi Y, Doi M, Uchiyama S, Nakazawa T, Nishiuchi Y, Yoshida T, Ohkubo T, Kobayashi Y
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Journal Title
J Phys Chem B.
Volume: 116
Issue: 23
Pages: 6908-6915
DOI
Related Report
Peer Reviewed
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[Journal Article] The triple helical structure and stability of collagen model peptide with 4(S)-hydroxyprolyl-pro-gly units2011
Author(s)
Motooka D, Kawahara K, Nakamura S, Doi M, Nishi Y, Nishiuchi Y, Kee Kang Y, Nakazawa T, Uchiyama S, Yoshida T, Ohkubo T, Kobayashi Y
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Journal Title
Biopolymers
Volume: 98
Issue: 2
Pages: 111-121
DOI
Related Report
Peer Reviewed
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