Chondroitinase ABC from Proteus vulgaris

The enzyme has been used to study the consequences of inducing acute, long-lasting changes in chondroitin sulfate proteoglycans using adult rat brain cells. Glycosaminoglycans have been digested with chondroitinase ABC for chondroitin/dermatan sulfate quantitation in keratocyte cell cultures obtained from fresh bovine corneal stromae.

Chondroitinase ABC catalyzes the eliminative degradation of polysaccharides containing (1-4)-β-D-hexosaminyl and (1-3)-β-D-glucuronosyl or (1-3)-α-L-iduronosyl linkages to disaccharides containing 4-deoxy-β-D-gluc-4-enuronosyl groups. It acts on chondroitin 4-sulfate, chondroitin 6-sulfate, and dermatan sulfate, and acts slowly on hyaluronate. The molecular weight is found to be approximately 120 kDa with 2 non-identical subunits of molecular masses 86 kDa and 32 kDa. The pH optimum is found to be 8.0 with chondroitin sulfate and 6.8 with hyaluronic acid and temperature optimum is 37 °C. 1 mM Zn²⁺ acts as an inhibitor, while 0.05 M acetate is an activator of the enzyme.

Contains potassium phosphate buffer salts and stabilizer

One unit will liberate 1.0 μmole of a mixture of 2-acetamido-2-deoxy-3-O-(β-D-gluc-4-ene-pyranosyluronic acid)-4-O-sulfo-D-galactose and 1.0 μmole of 2-acetamido-2-deoxy-3-O-(β-D-gluc-4-ene-pyranosyluronic acid)-6-O-sulfo-D-galactose from chondroitin sulfate from shark cartilage, per min at pH 8.0 at 37 °C.

View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer

Packages based on chondroitinase C activity.

Affinity purified