Amino Acid Composition and Physicochemical Characterization of Chondroitinase from Arthrobacter aurescens

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Abstract
The amino acid and carbohydrate compositions of chondroitinase AC [EC 4.2. 2.5] from Arthrobacter aurescens were determined, and its physicochemical properties were examined. 1. The enzyme has been shown to be a glycoprotein containing mannose, glucose, glucosamine, and glucuronic acid (3: 5: 4: 2). 2. Its molecular weight was estimated to be 76, 000 by gel filtration on Sephadex G-200, 75, 000–80, 000 by SDS disc electrophoresis, and 75,800 by sedimentation velocity. No subunits were detected in the molecule. 3. The physicochemical properties determined include: sedimentation coefficient (w=5.14S), diffusion constant (D0=6.09×10−7 cm2/sec), frictional ratio (f: f0=1.19) and apparent partial specific volume (v=0.73 ml/g). 4. The optical rotatory dispersion and circular dichroism of the enzyme were investigated. The contents of α-helix and β-structure of the enzyme were estimated to be 16 and 25%, respectively.