“…This is commonly accomplished by proteolytic or alkaline digestion of tissue or extracted proteoglycan. However, during these isolation procedures, the glycosaminoglycan chains may be degraded, and the average molecular weight and size distribution of the final product may, therefore, be lower and have a wider distribution of molecular sizes than those occurring in vivo (Robert et al, 1962;Whistler & Rowell, 1966;Blumberg & Ogston, 1957, 1958. On the other hand the preparative procedure may not be effective in degrading the protein core of the proteoglycan complex and the resulting glycosaminoglycan product will then have a higher average molecular weight and a broader size distribution than will free glycosaminoglycan chains (Luscombe & Phelps, 1967;Mathews, 1971).…”