Collagen Type I, salmon

Type I Collagen usually exists as a heterotrimer formed by alpha 1(I) and alpha 2(I) chains and is found in bone, cornea, skin and tendon. In foetal tissues also homotrimers of alpha-1(I) are found, but they are not constituents of normal adult tissues. Collagens consist of a family of highly specialized glycoproteins of which at least 16 genetically distinct types are known to date. The basal unit of a collagen molecule consists of a triple-helical structure formed by 3 alpha-chains. Predominant amino acids are glycine, proline and hydroxproline. Regularly also lysines and hydroxylysines occur, which are responsible for cross-linkage and glycosylation of the protein chains. Different composition of alpha-chains and different glycosylation contribute to the high variability of collagens in different tissues and organs. Salmon (Salmon salar) Collagen type I.