Nagamalleswari D, Joseph K T
Biochemistry Department Central Leather Research Institute, Madras, India.
Biochem Int. 1990 Dec;22(6):1041-51.
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.
对康氏躄鱼（S. commersonianus）肌隔膜胶原蛋白的生化组成和分子结构进行了研究。肌隔膜胶原蛋白的酸溶性更高（89.3%）。甘氨酸占肌隔膜氨基酸残基的近三分之一，与大鼠尾腱胶原蛋白相比，脯氨酸和羟脯氨酸的含量较低。在鱼类肌隔膜胶原蛋白中，清晰检测到两条不同的链，α1和α2，以及它们的交联成分β11和β12，这是I型胶原蛋白的典型特征。
