The effects of proteolytic enzymes on the hyaluronic acid complex of ox synovial fluid

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Abstract
Activated papain attacks the protein component of the hyaluronic acid complex of ox synovial fluid, leading to removal of protein from the polysaccharide. Papain inhibited with mercuric chloride or iodoacetamide, chymotrypsin and trypsin are inactive. Proteolysis causes a strong reduction of the non-Newtonian viscosity of solutions of the complex, while having relatively little effect on the viscosity measured at high velocity gradients. The sedimentation rate is lowered, and the average particle weight is reduced fivefold. The character of the mucin clot formed by hyaluronic acid complex with protein at acid pH is altered by treatment with papain. It is concluded that protein, in complex with hyaluronic acid, is essential to its maintenance in the state in which it occurs in synovial fluid in vivo.