Physico chemical studies on the myocommata of the fish Scomberoides commersonianus.

The biochemical composition and molecular organization of myocommata collagen in the fish S. commersonianus has been investigated. The myocommata collagen was more acid soluble (89.3%). Glycine makes up close to one third of the amino acid residues in myocommata with proline and hydroxyproline being lower as compared to rat tail tendon collagen. In fish myocommata collagen two distinct chains, alpha 1 and alpha 2 were clearly detected along with their crosslinked components beta 11 and beta 12, typical of type I collagen.