Cartilage, collagen

Collagen type 11 90-98% of total articular cartilage collagen. Composed of three a1(ll) chains. 

Yonath, A., and Traub, W. (1975). Crystallization of cyanogen bromide peptides from chick cartilage collagen. FEBS Lett. 57, 93-95. 

Figure 3.24. Diagram of the collagen fibrils in cartilage, collagen fibrils in cartilage are composed of a core of types XI and II collagen with zone type IX on the surface. Collagen fibrils are connected to each other and to the cell surface by proteoglycans.

Figure 3.27. Diagram illustrating split line pattern in articular cartilage. Collagen fibrils are oriented approximately parallel to the split lines in cartilage.

Salmon skin or cartilage collagen has been used as food additives, in tablets or powders. Carefully prepared salmon skin collagen is also used as gel for cell growth, since it yelds higher performance than porcine collagen. 

When extracting chondroitin sulfate from salmon head cartilage, collagen inevitably accompanies it. In this extraction process, from a pharmaceutical point of view, collagen is considered as an impurity. This is a kind of contradiction because if we administrate chondroitin sulfate and collagen simultaneously, the result will be beneficial and effective. Most marine bioresources contain many health beneficial compounds even in the same tissues. For this reason, we should design sequential extraction processes of those useful compounds from the most value added to the poorly valued compounds. For example, the first step for pharmaceutical use should be the mild extraction of compounds. And the final step should extract materials for fertilizers. 

Proteo-Glycosaminoglycan Core Proteins and Cartilage Collagens... 

Butler, W.T. (1970) Chemical Studies on the Cyanogen Bromide Peptides of Rat Skin Collagen. The Covalent Structure of al-CB5, the Major Hexose-containing Cyanogen Bromide Peptide of a V, Biochemistry, 9, 44-50 Butler, W.T., Finch, K.E. Miller, E.J. (1977) Covalent Structure of Cartilage Collagen. Amino Acid Sequence of Residues 363-551 of bovine al (II) Chains , Biochemistry, 16, 4981-90... 

Forsee, W.T., Springfield, J.D. Schutzbach, J.S. (1982) Effects of Phospholipids on al,2-Mannosidase Activity , Journal of Biological Chemistry, 257, 9963-7 Francis, G., Butler, W.T. Finch, J.E. (1978) The Covalent Structure of Cartilage Collagen. Amino Acid Sequence of Residues 552-661 of Bovine al (11) Chains , Biochemical Journal, 175, 921-30... 

Mandal, A. B. Ramesh, D. V. Dhar, S. C. Physicochemical studies of Micelle formation on sepia cartilage collagen solutions (pepsin extracted) in acetate buffer and its interaction with ionic and nonionic micelles Hydrodynamic and thermodynamic studies, PEBS, Eur.. Biochem., 1987,169, 617-628. 

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