Characterization of the skin collagen of a surface water fish Scomberoides commersonianus.
The molecular organization of the skin collagen in the fish S. commersonianus has been investigated. The contents of imino acids proline and hydroxyproline are less in the skin collagen. The major collagenous component of fish skin is homologous to type I collagen. The number of CNBr peptides in fish skin collagen alpha 1 chains is two times that of rat skin alpha 1 CNBr peptides. The proline-hydroxyproline ratio in the six peptides studied was 1.66-3.5 as compared to that of rat skin collagen (0.67-1.94). This indicates that proline and hydroxyproline are not uniformly distributed in the collagen molecule in fish skin collagen.
Nagamalleswari
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Biochemistry Department, Central Leather Research Institute, Adyar, Madras, India.
Joseph
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D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002852:Chromatography, Ion Exchange; D003094:Collagen / Q000032:analysis / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D005399:Fishes / Q000378:metabolism*; D006909:Hydroxyproline / Q000032:analysis; D008969:Molecular Sequence Data; D011392:Proline / Q000032:analysis; D011487:Protein Conformation; D051381:Rats; D012867:Skin / Q000737:chemistry*; D012995:Solubility
D000596:Amino Acids; D003094:Collagen; D011392:Proline; D006909:Hydroxyproline