Studies on fish scale collagen of Pacific saury (Cololabis saira)

Hideki Mori, Yurie Tone, Kouske Shimizu, Kazunori Zikihara, Satoru Tokutomi, Tomoaki Ida, Hideshi Ihara, Masayuki Hara

Research output: Contribution to journalArticlepeer-review

47 Citations (Scopus)


We purified and characterized Type I collagen from the scales of the Pacific saury (Cololabis saira) and compared it with collagen from other organisms. Subunit composition of C. saira collagen (2α1 + α2) was similar to that of red sea bream (Pagrus major) and porcine collagen. C. saira collagen did not form a firm gel after neutralization of pH in solution. The temperature of denaturation (24-25 °C) of C. saira collagen was slightly lower than that of P. major collagen (26-27 °C). The contents of proline and hydroxyproline were lower in red sea bream and Pacific saury collagen than in porcine collagen. Circular dichroism spectra and Fourier-transformed infrared spectra showed that heat denaturation caused unfolding of the triple helices in all three collagens.

Original languageEnglish
Pages (from-to)174-181
Number of pages8
JournalMaterials Science and Engineering C
Issue number1
Publication statusPublished - 2013 Jan 1
Externally publishedYes


  • Collagen
  • Denaturation temperature
  • Fibril
  • Fish scale
  • Gel
  • Pacific saury

ASJC Scopus subject areas

  • Materials Science(all)
  • Condensed Matter Physics
  • Mechanics of Materials
  • Mechanical Engineering


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