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E. Chung and E. J. Miller, “Collagen Polymorphism: Characterization of Molecules with the Chain Composition [α1(III)]3 in Human Tissues,” Science, Vol. 183, No. 4130, 1974, pp. 1200-1201.

has been cited by the following article:

• TITLE: Characterization of Acid-Soluble Collagen from Skins of Surf Smelt (Hypomesus pretiosus japonicus Brevoort)

  AUTHORS: Takeshi Nagai

  KEYWORDS: Attenuated Total Reflectance-Fourier Transform Infrared (ATR-FTIR) Analysis, Collagen, Denaturation Temperature, Skin, Surf Smelt

  JOURNAL NAME: Food and Nutrition Sciences, Vol.1 No.2, November 3, 2010

  ABSTRACT: 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.