E2039
Chondroitinase AC from Flavobacterium heparinum
recombinant, expressed in E. coli, ≥200 units/mg protein, For Chondroitin Sulfate Analysis
Synonym(s):
Chondroitin AC lyase
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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Product Name
Chondroitinase AC from Flavobacterium heparinum, recombinant, expressed in E. coli, ≥200 units/mg protein, For Chondroitin Sulfate Analysis
recombinant
expressed in E. coli
conjugate
(Glucosaminoglycan)
assay
≥90% (SDS-PAGE)
form
lyophilized solid
specific activity
≥200 units/mg protein
shipped in
dry ice
storage temp.
−20°C
Quality Level
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Application
Chondroitinase AC from Flavobacterium heparinum is an enzyme that cleaves sulfated and non-sulfated polysaccharide chains with (1-4) linkages between hexosamines and glucuronic acid residues, by an elimination mechanism. The resulting oligosaccharide products are mainly disaccharides with unsaturated uronic acids. Chondroitinase AC specifically degrades chondroitin sulfates A and C, but not chondroitin sulfate B (dermatan sulfate).
Chondroitinase AC has been applied to the analysis of chondroitin sulfate in commercial samples such as dietary supplements.
Highly purified to remove interferring β-glucuronidase and protease activities for use in the hydrolysis of chondroitin sulfate pror to HPLC analysis.
Other Notes
1 unit is defined as the amount of enzyme that will liberate 1.0 μmole per minute of unsaturated disaccharides from chondroitin sulfate A at pH 6.7 at 37 °C as measured by the change in A232. The εμΜ for the reaction product Δ-Di-4S (chondroitin sulfates A and B) is 5.1 and 5.5 for Δ-Di-6S (chondroitin sulfate C).
View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer
Storage Class
11 - Combustible Solids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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Determination of Chondroitin Sulfate Content in Raw Materials and Dietary Supplements by High-Performance Liquid Chromatography with Ultraviolet Detection After Enzymatic Hydrolysis: Single-Laboratory Validation
Ji, D., et al.
Journal - Association of Official Analytical Chemists, 90(3), 659-669 (2007)
Fernanda L Paganelli et al.
International journal of antimicrobial agents, 49(3), 355-363 (2017-02-12)
Enterococcus faecium is a multidrug-resistant (MDR) nosocomial pathogen causing significant morbidity in debilitated patients. New antimicrobials are needed to treat antibiotic-resistant E. faecium infections in hospitalised patients. E. faecium incorporates lipoteichoic acid (LTA) (1,3-polyglycerol-phosphate linked to glycolipid) in its cell
E M Denholm et al.
European journal of pharmacology, 416(3), 213-221 (2001-04-06)
In the current study, two specific glycosaminoglycan lyases, chondroitinase AC and chondroitinase B, were utilized to examine the roles of chondroitin sulfates and dermatan sulfate in tumor metastasis and angiogenesis. Melanoma cells (SK-MEL) or endothelial cells were treated with either
J Féthière et al.
Acta crystallographica. Section D, Biological crystallography, 54(Pt 2), 279-280 (1998-10-08)
Chondroitinase AC (E.C. 4.2.2.5) overexpressed in its host, Flavobacterium heparinum, was crystallized by vapor diffusion using polyethylene glycol methyl ether as precipitant. It crystallizes in the space group P43212 or its enantiomorph with a = b = 87.1 and c
Thomas N Huckerby et al.
The FEBS journal, 272(24), 6276-6286 (2005-12-13)
Chondroitin and dermatan sulfate (CS and DS) chains were isolated from bovine tracheal cartilage and pig intestinal mucosal preparations and fragmented by enzymatic methods. The oligosaccharides studied include a disaccharide and hexasaccharides from chondroitin ABC lyase digestion as well as
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