ABSTRACT
The preparation of native Type II molecules is complicated by the fact that cartilage collagen is highly insoluble. The isolation of Type II collagen is complicated by the observation that hyaline cartilage contains minor amounts of several collagenous chains different from α1(II). In order to determine the quality of the Type II collagen obtained in this way, the authors have employed several standard techniques. The amino acid analysis shows a composition typical of collagen, with one third of the residues being glycine. The nomenclature for the chains of various members of the collagenfamilies is derived from the observation that the α1(II)-chains of cartilage collagen elute from CM-cellulose columns in a position similar to α1(I)-chains of skin and bone (Type I) collagen and different from α2-chains. In summary, the simple procedure can be used to obtain Type II collagen of high purity in rather large quantities.
