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Chondroitinase B
Chondroitinase B cleaves dermatan sulfate.
Non-clinical applications :
- Research reagent (glycobiology, preparation of oligosaccharide libraries from dermatan sulfate).
Potential clinical applications:
- Scleroderma and pulmonary fibrosis are among a collection of fibroproliferative disorders. Cells proliferate in response to growth factors (GF) present in serum or produced by neighboring cells. The response of cells to GF is controlled by receptors and dermatan sulfates located on the cell surface. Chondroitinase B can remove dermatan sulfates on the surface of fibroblasts, thereby potentially decreasing the explosive and uncontrolled growth of these cells.
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| Chondroitinase B |
Data Sheet
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Synonyms |
Chondroitin B eliminase
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Source |
Flavobacterium heparinum (recombinant)
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EC Number |
E.C. 4.2.2.19
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Catalyzed Reaction |
The enzyme cleaves, via an elimination mechanism, polysaccharide chains containing 1-4 linkages between hexosamines and iduronic acid residues in dermatan sulfate (chondroitin B).The reaction yields oligosaccharide products (mainly disaccharides) containing unsaturated uronic acids which can be detected by UV spectroscopy at 232 nm.
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Substrate Specificity |
Dermatan sulfate (chondroitin sulfate B).
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Properties |
- Molecular weight: 54,779
- Isoelectric point: 9.4 – 9.6
- pH optimum for activity: 7 - 8
- pH range for activity: 5 - 10
- Optimal temperature range: 20 ° C – 37 ° C
- Crystal structure has been determined and published (see references).
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Purity |
≥ 90 % by reversed phase HPLC analysis.

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Specific Activity |
≥550 IU/mg (substrate: dermatan sulfate)
One international unit (IU) is defined as the amount of enzyme that will liberate 1.0 µmole unsaturated oligosaccharides from dermatan sulfate per minute at 30 ° C and pH 8.0.
>90 IU/mg (substrate: dermatan sulfate)
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Stability |
PN 50-018: 18 months frozen at – 70 ° C in aqueous buffers containing Sodium Phosphate and Sucrose 5%.
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Applications |
- As research reagent (glycosaminoglycan degradation).
- For the preparation of di- and oligo-saccharides of dermatan sulfate.
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Availability |
A proprietary expression system for F. heparinum and the fermentation and isolation processes developed by IBEX Pharmaceuticals allow the production of large quantities of high purity product. |
References
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- Review: "Enzymatic Degradation of Glycosaminoglycans". S. Ernst et al. in Critical Reviews in Biochemistry and Molecular Biology (1995), 30(5): 387-444.
- "Isolation and Expression in Escherichia coli of cslA and cslB, Genes Coding for the Chondroitin Sulfate-Degrading Enzymes Chondroitinase AC and Chondroitinase B, Respectively, from Flavobacterium heparinum". A.L. Tkalec, D. Fink, F. Blain, G. Zhang-Sun, M. Laliberté, D.C. Bennett, K. Gu, J.J.F. Zimmermann and H. Su, in Applied and Environmental Microbiology (2000) 66(1): 29-35.
- "Purification, Characterization and Specificity of Chondroitin Lyases and Glycuronidase from Flavobacterium heparinum". K. Gu, R.J. Linhardt, M. Laliberté, K. Gu and J. Zimmermann, in Biochem. J. (1995) 312: 569-577.
- "A comparative Study Between a Chondroitinase B and a Chondroitinase AC from Flavobacterium heparinum". M.Y.M. Michelacci and D.C.P. Dietrich, in Biochemical Journal (1975) 151: 121-129.
- "Crystal Structure of Chondroitinase B from Flavobacterium heparinum and its Complex with a Disaccharide Product at 1.7 Å Resolution". W. Huang, A. Matte, Y. Li, Y.S. Kim, R.J. Linhardt, H. Su and M. Cygler, in J. Mol. Biol. (1999) 294: 1257-1269.
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