• 1 January 1977
    • journal article
    • research article
    • Vol. 123  (APR) , 437-457
Abstract
Blocks of collagen fibrils were prepared from human articular cartilage employing 2 techniques which selectively remove either the proteoglycans or both the proteoglycans and collagen fibrils of the non-calcified cartilage layer. Amino acid analysis of the resultant collagen fibrils confirmed the purity of the collagen. Blocks of cartilage were observed by scanning electron microscopy in 4 orientations: normal to the articular surface; in section; the cleaved surface of blocks which were broken in a plane parallel to the artificial splits that were generated by the insertion of a pin; and the calcified collagen fiber structure down to the subchondral bone trabeculae. Five features of the organization of the collagen fibrils were observed and were discussed in relation to previously proposed structures for cartilage.