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C3667

Sigma-Aldrich

Chondroitinase ABC from Proteus vulgaris

BSA free, lyophilized powder, specific activity 50-250 units/mg protein

Synonyma:

4.2.2.20, 4.2.2.21, Chondroitin ABC Lyase

Přihlásitk zobrazení cen stanovených pro organizaci a smluvních cen
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About This Item

Číslo CAS:
9024-13-9
Číslo enzymu podle klasifikace EK:
4.2.2.4 (BRENDA, IUBMB)
EC Number:
232-777-9
MDL number:
MFCD00130795
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

bacterial (Proteus vulgaris)

Quality Level

300

conjugate

(Glucosaminoglycan)

form

lyophilized powder

specific activity

50-250 units/mg protein

mol wt

120 kDa by gel filtration

composition

Protein, ~10% Lowry

solubility

0.01% bovine serum albumin aqueous (BSA) solution: soluble

application(s)

diagnostic assay manufacturing

foreign activity

protease, essentially free

storage temp.

−20°C

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Application

The enzyme has been used to study the consequences of inducing acute, long-lasting changes in chondroitin sulfate proteoglycans using adult rat brain cells. Glycosaminoglycans have been digested with chondroitinase ABC for chondroitin/dermatan sulfate quantitation in keratocyte cell cultures obtained from fresh bovine corneal stromae.

Biochem/physiol Actions

Chondroitinase ABC catalyzes the eliminative degradation of polysaccharides containing (1-4)-β-D-hexosaminyl and (1-3)-β-D-glucuronosyl or (1-3)-α-L-iduronosyl linkages to disaccharides containing 4-deoxy-β-D-gluc-4-enuronosyl groups. It acts on chondroitin 4-sulfate, chondroitin 6-sulfate, and dermatan sulfate, and acts slowly on hyaluronate. The molecular weight is found to be approximately 120 kDa with 2 non-identical subunits of molecular masses 86 kDa and 32 kDa. The pH optimum is found to be 8.0 with chondroitin sulfate and 6.8 with hyaluronic acid and temperature optimum is 37 °C. 1 mM Zn2+ acts as an inhibitor, while 0.05 M acetate is an activator of the enzyme.

Packaging

Packages based on chondroitinase C activity.

Other Notes

Contains potassium phosphate buffer salts and stabilizer
View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer

Unit Definition

One unit will liberate 1.0 μmole of a mixture of 2-acetamido-2-deoxy-3-O-(β-D-gluc-4-ene-pyranosyluronic acid)-4-O-sulfo-D-galactose and 1.0 μmole of 2-acetamido-2-deoxy-3-O-(β-D-gluc-4-ene-pyranosyluronic acid)-6-O-sulfo-D-galactose from chondroitin sulfate from shark cartilage, per min at pH 8.0 at 37 °C.

Preparation Note

Affinity purified

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)

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Osvědčení o analýze (COA)

Lot/Batch Number
0000198322
0000376887
0000376885
0000198322
0000376887

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P N Bansal et al.
Osteoarthritis and cartilage, 18(2), 184-191 (2009-10-10)
An early hallmark of osteoarthritis (OA) is the progressive loss of glycosaminoglycans (GAGs), the extracellular matrix (ECM) component of articular cartilage that confers it with compressive stiffness. Our aim in this work is to establish the feasibility of using Contrast
Susan M Smith et al.
International journal of molecular sciences, 20(3) (2019-01-27)
The aim of this study was to assess if the ovine articular cartilage serine proteinase inhibitors (SPIs) were related to the Kunitz inter-α-trypsin inhibitor (ITI) family. Ovine articular cartilage was finely diced and extracted in 6 M urea and SPIs
Elizabeth J Bradbury et al.
Brain research bulletin, 84(4-5), 306-316 (2010-07-14)
Chondroitin sulphate proteoglycans (CSPGs) are potent inhibitors of growth in the adult CNS. Use of the enzyme chondroitinase ABC (ChABC) as a strategy to reduce CSPG inhibition in experimental models of spinal cord injury has led to observations of a
G Brückner et al.
Experimental brain research, 121(3), 300-310 (1998-09-24)
Lattice-like perineuronal accumulations of extracellular-matrix proteoglycans have been shown to develop during postnatal maturation and to persist throughout life as perineuronal nets (PNs) in many brain regions. However, the dynamics of their reorganization in adults are as yet unknown. The
Rong-Rong Zhao et al.
Neuroscience bulletin, 29(4), 477-483 (2013-07-11)
After spinal cord injury (SCI), re-establishing functional circuitry in the damaged central nervous system (CNS) faces multiple challenges including lost tissue volume, insufficient intrinsic growth capacity of adult neurons, and the inhibitory environment in the damaged CNS. Several treatment strategies
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