Purification and properties of the enzyme chondroitinase.

The enzymatic degradation of chondroitin sulfuric acid can be catalyzed by purified bovine testicular hyaluronidase (1, 2) and by an enzyme preparation from Flavobacterium heparinum (3). Dodgson and Lloyd (4) obtained a chondroitinase from Proteus vulgaris that converted chondroitin sulfuric acid to the disaccharide, N-acetylchondrosin sulfate. Previous work from this laboratory (5) has confirmed and extended the observations of Dodgson and Lloyd. In these studies two disaccharides were isolated from the enzyme reaction and identified as N-acetylchondrosin and N-acetylchondrosin sulfate (5). Studies on the purification and properties of the Proteus vulgaris chondroitinase are presented in this report.