C3667
Chondroitinase ABC from Proteus vulgaris
BSA free, lyophilized powder, specific activity 50-250 units/mg protein
Synonym(s):
4.2.2.20, 4.2.2.21, Chondroitin ABC Lyase
Sign Into View Organizational & Contract Pricing
All Photos(4)
About This Item
Recommended Products
biological source
bacterial (Proteus vulgaris)
Quality Level
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
Looking for similar products? Visit Product Comparison Guide
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 Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Customers Also Viewed
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
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
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
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
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service