Pharmaceutical compositions of chondroitinase ABC isolated from Proteus vulgaris ATCC 6896

Abstract

A crystallizable, purified chondroitinase ABC having a molecular weight of about 100,000 dalton by the measurement of the SDS-polyacrylamide gel electrophoresis (SDS-PAGE) and the measurement by the gel permeation chromatography method, having alanine as the N-terminal amino acid and proline as the C-terminal amino acid is disclosed. A process for the purification of the crystallizable purified chondroitinase ABC comprising removing nucleic acid from an surfactant solution extract obtained from cells of chondroitinase ABC-producing microorganisms and chromatographically treating by concentration gradient elution using a weak cation exchange resin or a strong cation exchange resin is disclosed. A composition comprising a chondroitinase and serum albumin, gelatin, or a nonionic surfactant is used to treat disc displacement. The enzyme is isolate from Proteus vulgaris ATCC 6896.

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