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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