The objectives of the project remains the study of the physiologic role of cartilage lysozyme. Our recent findings indicate that a certain pool of cartilage lysozyme is selectively associated with hyaluronic acid forming a complex of such a nature that it cannot be broken by dissociative solvents such as 4 M guanidinium hydrochloride in cesium chloride density gradients. It is, therefore, postulated that lysozyme can occupy certain proteoglycan-binding sites on the hyaluronic acid molecule thereby regulating the size and/or degree of aggregation of the proteoglycan-aggregates. Furthermore, emphasis will be directed toward a detailed study of this hyaluronic acid-lysozyme complex by applying selective degradation of hyaluronic acid by Streptomyces derived hyaluronidase. In addition, we were able to show that the "blockage" of freshly sythesized lysozyme with either anti-lysozyme antibodies or soluble chitin oligomers inhibited the biosynthesis of matrix components such as proteoglycans. These data will be substantiated to show that lysozyme plays and essential role in cartilage extracellular matrix biosynthesis and organization.