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Merck

C2780

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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Número CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
Número CE:
MDL number:
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Nombre del producto

Condroitinasa AC from Flavobacterium heparinum, lyophilized powder, 0.5-1.5 units/mg protein (using chondroitin sulfate A as substrate)

conjugate

(Glucosaminoglycan)

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

Quality Level

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Other Notes

Contains potassium phosphate buffer salts and BSA as stabilizer.
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).

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

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).

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.

Clase de almacenamiento

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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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
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
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
Nicola Volpi et al.
Glycobiology, 19(4), 356-367 (2008-12-06)
Glycosaminoglycans from the body of marine clam Scapharca inaequivalvis were extracted at about 0.15- 0.18 mg/g of dry tissue, composed of dermatan sulfate (DS) (approx. 74%) and heparan sulfate (26%). After treatment with nitrous acid, DS was isolated for further

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