Amino acid composition and physiochemical characterization of chondroitinase from Arthrobacter aurescens.

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 wieght 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 veolcity. No subunits were detected in the molecule. 3. The physicochemical properties determined include: sedimentation coefficient (s(o)20, w=5.14 S), diffusion constant (D(o)=6.09 X 10(-7) cm2/sec), frictional ratio (f:f(o)=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 alpha-helix and beta-structure of the enzyme were estimated to be 16 and 25%, respectively.