Acid-soluble collagen was extracted from the skins of surf smelt and characterized. The yield of collagen was high about 24.0% on a dry weight basis. By SDS-polyacrylamide gel electrophoresis and CM-Toyopearl 650 M column chromatography, this collagen is a heterotrimer with a chain composition of α1α2α3. The denaturation temperature was 32.5℃, about 4.5℃ lower than that from porcine skin. Attenuated total reflectance-fourier transform infrared analysis showed that the percentage of secondary structural components in this collagen were 11% α-helix, 34% β-sheet, 19% β-turn, and 21% others. It suggests that the triple helical structure is present in the acid-soluble collagen from the skins of the surf smelt in comparison to that from the skin of porcine.
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