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C2780

Sigma-Aldrich

Condroitinasa AC from Flavobacterium heparinum

lyophilized powder, 0.5-1.5 units/mg protein (using chondroitin sulfate A as substrate)

Sinónimos:

Condroitina AC liasa

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About This Item

Número de CAS:
9047-57-8
Comisión internacional de enzimas:
4.2.2.5 (BRENDA, IUBMB)
MDL number:
MFCD00130796
UNSPSC Code:
12352204
NACRES:
NA.54

conjugate

(Glucosaminoglycan)

Quality Level

200

form

lyophilized powder

specific activity

0.5-1.5 units/mg protein (using chondroitin sulfate A as substrate)

composition

Protein, ~15% Lowry

solubility

0.02 M phosphate buffer: soluble (pH 7.0)

foreign activity

Glycosaminoglycan (GAG) degradation enzymes, may contain trace amount

storage temp.

−20°C

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Application

Chondroitinase AC from Sigma has been used for the large scale preparation of glycosaminoglycan (GAG) fractions during the study of structural and sequence motifs in dermatan sulfate.
Chondroitinase AC has been applied to the analysis of chondroitin sulfate in commercial samples such as dietary supplements.

Biochem/physiol Actions

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).

Other Notes

Contains potassium phosphate buffer salts and BSA as stabilizer.
Véase más información sobre enzimas para análisis de carbohidratos complejos en www.sigma-aldrich.com/enzymeexplorer

Suitability

Depending on reaction conditions, digestion of chondroitin sulfate may result in hydrolysis of disaccharides

Unit Definition

One unit will cause a ΔA232 of 1.0 per minute due to the release of unsaturated disaccharide from chondroitin sulfate A at pH 7.3 at 37 °C. Reaction volume: 3.1 ml (light path 1 cm).

Preparation Note

Reconstitute the product in 20 mM phosphate buffer, pH 7.0. Subsequent dilutions can be made with a 0.01% aqueous bovine serum albumin solution.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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C B Knudson et al.
The Journal of cell biology, 100(5), 1753-1758 (1985-05-01)
Hyaluronate levels change dramatically during morphogenesis of various tissues and organs. Morphological detection of the exact temporal and spatial distribution patterns of hyaluronate may help to elucidate its role in morphogenesis. Since no specific direct method for visualizing hyaluronate with
S P Levine et al.
Blood, 75(4), 902-910 (1990-02-15)
Platelet factor 4 (PF4) is a hydrophobic, alpha-granule protein with potent antiheparin activity. It also binds to a chondroitin sulfate-containing proteoglycan (PG) isolated from platelets. In order to evaluate further the relationship between PF4 and the chondroitin sulfate-containing proteoglycan in
Florian D Naal et al.
Journal of biomedical materials research. Part B, Applied biomaterials, 87(1), 19-25 (2008-03-25)
Meniscal allograft processing procedures, in particular gamma irradiation, deteriorate the biomechanical and biological properties of the transplanted tissue. High hydrostatic pressure (HHP) treatment, widely used in food technology to inactivate microorganisms while preserving natural compounds, might serve as a gentle
E B Hunziker
Osteoarthritis and cartilage, 9(1), 22-32 (2001-02-17)
We have previously shown (Hunziker and Rosenberg, J Bone Joint Surg 1996;78A:721-33) that synovial cells can be induced to migrate into partial-thickness articular cartilage defects, therein to proliferate and subsequently to deposit a scar-like tissue. We now wished to ascertain
Studies on the enzyme chondroitinase: product structure and ion effects.
H I NAKADA et al.
Archives of biochemistry and biophysics, 94, 244-251 (1961-08-01)
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