Chondroitinase ABC isolated from proteus vulgaris ATCC 6896

Details Chondroitinase ABC isolated from proteus vulgaris ATCC 6896 Chondroitinase ABC isolated from proteus vulgaris ATCC 6896

1993-06-23

1996-03-05

Naff, David M.

Chemistry: molecular biology and microbiology

Enzyme , proenzyme; compositions thereof; process for...

Lyase

435873, 4352521, 424 945, C12N 988, C12N 112, C01G 1704

Patent

active

054967180

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. 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. A composition comprising a chondroitinase and serum albumin, gelatin, or a nonionic surfactant. The chondroitinase ABC is isolated from Proteus vulgaris ATCC 6896.

REFERENCES:
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patent: 5198355 (1993-03-01), Kikuchi et al.
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Sato et al., Biotechnol. & Bioengineering, vol. 28, 1707-1712, 1986.
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Sato, et al., "Subunit Structure of Chondroitinase ABC from Proteus vulgaris", Agric. Biol. Chem.,50(4):1057-1059 (1986).

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