Sigma-Aldrich Chondroitinase ABC from Proteus vulgaris. lyophilized powder, 0.3-3 units/mg solid. 5 units

Chondroitinase ABC from Sigma has been used to digest O-linked chondroitin sulfate-like glycosaminoglycan (CSGAG).[1] The enzyme has also been used to digest glycosaminoglycan chains in proteoglycans during the construction and expression of a recombinant versican gene in mammalian systems.[2] Furthermore, it has been used to digest chondroitin sulfate in the proteoglycan complexes.[3] The enzyme has also been used in the removal of glycan chains from aggrecan, which eliminates the axon growth-inhibitory effect of aggrecan.[4]

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. However, it acts slowly on hyaluronate. The molecular weight is approximately 120 kDa with 2 non-identical subunits of molecular masses 86 kDa and 32 kDa. The pH optimum is 8.0 with chondroitin sulfate and 6.8 with hyaluronic acid. The optimal temperature is 37 °C. 1 mm Zn²⁺ acts as an inhibitor, while 0.05 M acetate is an activator of the enzyme.

Packages based on chondroitinase C activity.

Lyophilized powder containing Tris buffer salts

Reconstitute in a 0.01% bovine serum albumin aqueous (BSA) solution. Subsequent dilutions can be made into a buffer containing 50 mm Tris, pH 8.0, with 60 mm sodium acetate and 0.02% BSA. Solutions should be freshly prepared.

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