Studies on fish scale collagen of Pacific saury (Cololabis saira) |
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Authors: | Hideki Mori Yurie Tone Kouske Shimizu Kazunori Zikihara Satoru Tokutomi Tomoaki Ida Hideshi Ihara Masayuki Hara |
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Affiliation: | Department of Biological Science, Graduate School of Science, Osaka Prefecture University, 1-2 Gakuen-cho, Naka-ku, Sakai, Osaka 599-8570, Japan |
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Abstract: | 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. |
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