Abstract
Chrondroitin sulphate and chondromuco-protein, isolated from cartilage, formed insoluble complexes with blood proteins, mainly fibrinogen and [beta]-lipoproteins, their composition depending on whether plasma or serum was used, the pH and the mucopolysaccharide concentration. Complexes isolated from human plasma contained [alpha]-, [beta]- and [gamma] -globulins, [beta]-lipoproteins, cholesterol, mucopolysaccharides, sialoproteins and components of the fibrinolytic system (fibrinogen, plasminogen and streptokinase proactivator). Incubation of the complexes with plasminogen activators (streptokinase and urokinase) formed caseinolytic, fibrinolytic and fibrinogenolytic plasmin. Partially degraded chondromucoprotein (for which the name "chondromucopeptide" is proposed), released in vitro and in vivo from rabbit cartilage by plasmin and papain respectively, formed insoluble complexes with rabbit plasma proteins. The complexes were qualitatively similar to certain pathological tissue deposits (fibrinoid, sclerotic, hyaline and amyloid material), and possible mechanisms for deposition are discussed.