Recent advances in collagen methodology have now permitted a detailed investigation of this major structural protein of articular cartilage. Collagen structure, metabolism, antl morphology have been extensively studied in "soft" connective tissues (1,Z). Tlie difficulty of collagen extraction from cartilage and bone has prevented its characterization in "hard" connective tissues until recently (3). Since September 3, 1974; accepted May 5, 1975. in the rapidly progressing field of articular cartilage collagen research.Articular cartilage is a highly specialized connective tissue consisting of relatively small numbers of cells distributed throughout abundant extracellular matrix. T h e biophysical properties of articular cartilage that allow joints to serve as bearings in locomotion are in part related to tlie unique composition of tlie extracellular matrix. Collagen constitutes approximately 10% of the wet and 50y0 of the dry weight of cartilage (5). Noncollagenous material constitutes approximately the other 507, of the dry mass of articular cartilage matrix, of which the bulk is in the form of heterogenous proteoglycan complexes (6). Rather than being a single compound, the proteoglycans comprise multiple compounds that differ from each other in their sulfate content, amino acicl sequence of the peptide core, glycosaminoglycan composition, and side chain length.T h e biomaterial properties of the cartilage are a consequence of the interaction of the collagen and proteoglycans in the extracellular matrix. T h e chain extensions of the proteoglycans antl the electrostatic charges provide the molecular basis for consequent mechanical matrix stiffness (7). Tlie inability of the sulfate moieties to diffuse away from the glycosaminoglycan side chains influences the partition of water and diffusible electrolytes (8,9). T h e interaction of the proteoglycan with collagen is necessary for them to behave like gels (7). Whether the interaction is chem-