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Information on EC 4.2.2.20 - chondroitin-sulfate-ABC endolyase and Organism(s) Proteus vulgaris and UniProt Accession P59807
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4.2.2.20 chondroitin-sulfate-ABC endolyaseIUBMB Comments
This enzyme degrades a variety of glycosaminoglycans of the chondroitin-sulfate- and dermatan-sulfate type. Chondroitin sulfate, chondroitin-sulfate proteoglycan and dermatan sulfate are the best substrates but the enzyme can also act on hyaluronan at a much lower rate. Keratan sulfate, heparan sulfate and heparin are not substrates. In general, chondroitin sulfate (CS) and dermatan sulfate (DS) chains comprise a linkage region, a chain cap and a repeat region. The repeat region of CS is a repeating disaccharide of glucuronic acid (GlcA) and N-acetylgalactosamine (GalNAc) [-4)GlcA(beta1-3)GalNAc(beta1-]n, which may be O-sulfated on the C-4 and/or C-6 of GalNAc and C-2 of GlcA. GlcA residues of CS may be epimerized to iduronic acid (IdoA) forming the repeating disaccharide [-4)IdoA(alpha1-3)GalNAc(beta1-]n of DS. Both the concentrations and locations of sulfate-ester substituents vary with glucosaminoglycan source . The related enzyme EC 4.2.2.21, chondroitin-sulfate-ABC exolyase, has the same substrate specificity but removes disaccharide residues from the non-reducing ends of both polymeric chondroitin sulfates and their oligosaccharide fragments produced by EC 4.2.2.20 .
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Word Map
- 4.2.2.20
- proteoglycans
- glycosaminoglycans
- heparan
- dermatan
- collagen
- cartilage
- hyaluronidase
- cord
-
hyaluronic
- heparitinase
-
cspgs
-
articular
- 4-sulfate
- scar
-
nitrous
-
35ssulfate
- decorin
-
alcian
- aggrecan
- keratanase
-
perineuronal
-
intervertebral
- biglycan
-
iduronic
- endo-beta-galactosidase
-
chemonucleolysis
-
monosulfated
- chondroitin-4-sulfate
- biotechnology
-
intradiscal
-
cetylpyridinium
- neurocan
- molecular biology
- versican
- chymopapain
-
fibrosus
-
sulfate-containing
- hexasaccharide
-
unsulfated
- medicine
-
6-sulphated
-
hemisection
- wisteria
-
oversulfated
-
hexuronic
- pulposus
-
stub
-
beta-d-xyloside
-
3hglucosamine
- brevican
-
undersulfated
- phosphacan
The taxonomic range for the selected organisms is: Proteus vulgaris
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
chondroitinase abc, chabc, chondroitinase abc i, ch'ase abc, ch'ase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
chondroitinase ABC
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Endolytic cleavage of (1->4)-beta-galactosaminic bonds between N-acetylgalactosamine and either D-glucuronic acid or L-iduronic acid to produce a mixture of Delta4-unsaturated oligosaccharides of different sizes that are ultimately degraded to Delta4-unsaturated tetra- and disaccharides
related enzyme EC 4.2.2.21
-
SYSTEMATIC NAME
IUBMB Comments
chondroitin-sulfate-ABC endolyase
This enzyme degrades a variety of glycosaminoglycans of the chondroitin-sulfate- and dermatan-sulfate type. Chondroitin sulfate, chondroitin-sulfate proteoglycan and dermatan sulfate are the best substrates but the enzyme can also act on hyaluronan at a much lower rate. Keratan sulfate, heparan sulfate and heparin are not substrates. In general, chondroitin sulfate (CS) and dermatan sulfate (DS) chains comprise a linkage region, a chain cap and a repeat region. The repeat region of CS is a repeating disaccharide of glucuronic acid (GlcA) and N-acetylgalactosamine (GalNAc) [-4)GlcA(beta1-3)GalNAc(beta1-]n, which may be O-sulfated on the C-4 and/or C-6 of GalNAc and C-2 of GlcA. GlcA residues of CS may be epimerized to iduronic acid (IdoA) forming the repeating disaccharide [-4)IdoA(alpha1-3)GalNAc(beta1-]n of DS. Both the concentrations and locations of sulfate-ester substituents vary with glucosaminoglycan source [5]. The related enzyme EC 4.2.2.21, chondroitin-sulfate-ABC exolyase, has the same substrate specificity but removes disaccharide residues from the non-reducing ends of both polymeric chondroitin sulfates and their oligosaccharide fragments produced by EC 4.2.2.20 [4].
CAS REGISTRY NUMBER
COMMENTARY
9024-13-9
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
chondroitin 6-sulfate
unsaturated chondroitin 6-sulfate disaccharide
-
-
-
-
?
chondroitin sulfate proteoglycan
?
-
70% of the rate with chondroitin-6-sulfate
-
-
?
additional information
?
-
-
no substrate: keratan sulfate, heparin, heparan sulfate. Enzyme produces a wide range of differently sized oligosaccharides. After exhaustive degradation, end products are tetra- and disaccharides
-
-
?
chondroitin 4-sulfate
?
-
a total of 13 oligosaccharides ranging in size from di- to tetradecasaccharides are identified. Oligosaccharides are composed of repeating unsaturated uronic acid (DELATA UA)-GalNAc disaccharide subunits, with up to the equivalent of one sulfate per disaccharide. Two types of oligosaccharide structures are identified: the first type has an even number of saccharide residues with DELTA(UA) at the nonreducing end and GalNAc at the reducing end and the second type is composed of an odd number of residues with UA at the reducing terminus. Number of sulfates associated with the oligosaccharides increases with the size of the oligosaccharide, up to the equivalent of one sulfate per disaccharide
-
-
?
chondroitin 4-sulfate
?
-
liquid chromatography-mass spectrometry is applied to determine the action pattern of different chondroitin lyases: products of chondroitinase ABC from Proteus vulgaris and chondroitinase AC from Flavobacterium heparinum contain unsaturated oligosaccharides of sizes ranging from disaccharide to decasaccharide, demonstrating that both are endolytic enzymes
-
-
?
dermatan sulfate
?
-
a total of 13 oligosaccharides ranging in size from di- to tetradecasaccharides are identified. Oligosaccharides are composed of repeating unsaturated uronic acid (DELATA UA)-GalNAc disaccharide subunits, with up to the equivalent of one sulfate per disaccharide. Two types of oligosaccharide structures are identified: the first type has an even number of saccharide residues with DELTA(UA) at the nonreducing end and GalNAc at the reducing end and the second type is composed of an odd number of residues with UA at the reducing terminus. Number of sulfates associated with the oligosaccharides increases with the size of the oligosaccharide, up to the equivalent of one sulfate per disaccharide
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.073
chondroitin sulfate A
recombinant protein fused to maltose-binding protein, pH 7.4, 50°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
587
chondroitin sulfate A
recombinant protein fused to maltose-binding protein, pH 7.4, 50°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3180
recombinant protein fused to maltose-binding protein, pH 7.4, 50°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Q140A
mutation improves both activity and thermal stability of the enzyme, and additionally improves resistance to trypsin degradation
Q140G
mutation improves both activity and thermal stability of the enzyme, and additionally improves resistance to trypsin degradation
additional information
additional information
engineering of a mammalian expression system of an epitope-tagged chondroitinase ABC protein. At the 5'-end, an optimized KOZAK-ATG sequence is inserted, to allow efficient eukaryotic translation, followed by a 60 base pair secretion sequence from the fish Oreochromis aureus, engineered for efficient crosshost recombinant protein expression. At the 3'-end, a 3xFlag epitope tag is added. The addition of the eukaryotic secretion signal sequence allows secretion, but interferes with function of the secreted enzyme. In contrast, expression of the chondroitinase ABC gene without N-terminal eukaryotic secretion sequence or bacterial hydrophobic leader sequence leads to efficient secretion of a biologically active chondroitinase ABC protein from both immortalized and primary cells. The C-terminal epitope tag can be utilized to follow expression of this protein
additional information
-
engineering of a mammalian expression system of an epitope-tagged chondroitinase ABC protein. At the 5'-end, an optimized KOZAK-ATG sequence is inserted, to allow efficient eukaryotic translation, followed by a 60 base pair secretion sequence from the fish Oreochromis aureus, engineered for efficient crosshost recombinant protein expression. At the 3'-end, a 3xFlag epitope tag is added. The addition of the eukaryotic secretion signal sequence allows secretion, but interferes with function of the secreted enzyme. In contrast, expression of the chondroitinase ABC gene without N-terminal eukaryotic secretion sequence or bacterial hydrophobic leader sequence leads to efficient secretion of a biologically active chondroitinase ABC protein from both immortalized and primary cells. The C-terminal epitope tag can be utilized to follow expression of this protein
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
in commercial preparations, there is a significant effect of lot and time on thermal stability. Average enzymatic activity is significantly decreased after 1 and 3 days at 39°C and 37°C, resp. The average activity seen after 1 day is significantly different between the two temperatures. Addition of bovine serum albumin preserves enzymatic activity at 1 day, but not 3 days, at 39°C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme catalytic activity and intrinsic fluorescence intensity increase in the presence of cosolvents glycerol, sorbitol and trehalose whereas no considerable conformational changes are observed in far-UV CD spectra. In the presence of trehalose a significant increase in meltin temperature is observed.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
25°C, 17 days, complete loss of activity, in presence of 1 M trehalose 85% residual activity after 21 days
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
fusion protein with maltose-binding protein, expression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
when expressed in a mammalian cell, residues N675, N515, N345, N338 and N282 are all glycosylated which prevents secretion of functional enzyme. Directed mutagenesis of selected N-glycosylation sites allows efficient secretion of active chondroitinase. Mutation if residue N751 renders the enzyme inactive. Mutations required for efficient secretion of active enzyme are those eliminating glycosylation at N282, N336, N345, and N515, and mutation of N675 increases the activity still further
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
bond strength of two etch-and-rinse adhesives to chondroitinase ABC treated dentin is investigated. Human extracted molars are treated with chondroitinase ABC. Increased mean values of microtensile bond strength and reduced nanoleakage expression are shown for both adhesives after chondroitinase ABC treatment of the dentin surface. This study supports the hypothesis that adhesion can be enhanced by removal of chondroitin 4/6 sulfate and dermatan sulfate, probably due to a reduced amount of water content and enlarged interfibrillar spaces
medicine
molecular biology
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glycosaminoglycans are extracted from cooked haddock muscle. Reverse phase chromatography and digestion with chondroitinase ABC (Chase) is used. FeCl3 is mixed with the purified glycosaminoglycans, and Fe uptake is measured by ferritin formation using an in vitro digestion/Caco-2 cell model. The identificative analyses suggest that chondroitin/dermatan sulfate-related structures promote Fe uptake by Caco-2 cells
medicine
-
masked intravitreal injection of chondroitinase, human or porcine plasmin into eye of pigs. Spontaneous posterior vitreous detachment occurs more frequently in human plasmin-treated and all plasmin treated eyes than in placebo controls. Treatment with chondroitinase fails to produce an effect
medicine
-
adult rats that undergo unilateral cervical spared-root lesion exhibit profound sensory deficits for 4 weeks after injury. Delivery of a focal intraspinal injection of the chondroitin sulfate proteoglycan-degrading enzyme chondroitinase ABC (ChABC) is sufficient to restore sensory function after lesion. In vivo electrophysiological recordings confirm that behavioral recovery observed in ChABC-treated rats is consequent on reorganization of intact C7 primary afferent terminals and not regeneration of rhizotomized afferents back into the spinal cord within adjacent segments. These data confirm that intact spinal circuits have a profound influence on functional restoration after spinal cord injury
medicine
-
antisense vimentin cDNA and ChABC are administered to hemisected rat spinal cords. Using RT-PCR, Western blotting and immunohistochemistry, it is shown that the combined treatment reduces the formation of glial scar and cystic cavities through degrading chondroitin sulfate proteoglycans molecules and inhibiting intermediate filament proteins
medicine
-
effects of degrading chondroitin sulfate glycosaminoglycan with Ch'ase ABC in the injured spinal cords of adult cats is assessed. Recovery of skilled locomotion (ladder, peg, and beam) is significantly accelerated in Ch'ase ABC-treated cats compared to controls. Ch'ase ABC-treated cats also show greater recovery of specific skilled locomotor features including intralimb movement patterns and significantly greater paw placement onto pegs. These findings show that intraspinal cleavage of CS GAGs can enhance recovery of function following spinal cord injury in large animals with sophisticated motor behaviors and axonal growth requirements similar to those encountered in humans
medicine
-
immediate and long-term effects of a single injection of chABC on chondroitin sulphate proteoglycans, chondroitin sulphate glycosaminoglycan and axon regeneration after unilateral nigrostriatal lesions in adult rats are investigated. In chABC-treated animals, the total chondroitin sulphate glycosaminoglycan remain at low level throughout the 28 day experimental period. This suggests the persistence of active chABC for at least 10 days after injection which is able to digest chondroitin sulphate proteoglycans released from cells during this time. Results suggest that a single injection of chABC can produce an environment conducive to CNS repair for over 10 days
medicine
-
it is shown that cervical spinal cord injury (SCI) results in the significantly increased expression of the chondroitin sulfate proteoglycans (CSPGs) NG2, neurocan, and brevican in the distant denervated dorsal column nuclei (DCN). The CSPGs present a potent barrier to reinnervation by regenerating axons from microtransplanted adult sensory neurons following SCI that can be overcome by chondroitinase ABC (chABC) application and increased neurotrophin-3 (NT-3) expression within the nucleus
medicine
-
rats with a crush in the dorsal funiculi of the C4 segment of the spinal cord are treated with chondroitinase ABC delivered to the lateral ventricle. Treatment is started at the time of injury or after a 2, 4 or 7 days delay. Behavioural testing over 6 weeks shows that acutely treated animals show improve skilled forelimb reaching compared to controls. Chondroitinase-treated animals show greater axon regeneration than controls. The treatment effect on contact placing, stride length and axon regeneration is not dependent on the timing of the start of treatment, but in skilled paw reaching acutely treated animals recover better function
medicine
-
topical injection of chondroitinase ABC after 15-mm tibial nerve resection can significantly increase the critical length of nerve gap repair by tubulization or artificial nerve placement
medicine
-
development of thermostabilized chondroitinase ABC and a system for its sustained local delivery in vivo, obviating the need for chronically implanted catheters and pumps. Presence of with 1M trehalose significantly enhances chondroitinase ABC thermal stability and prolongs enzyme activity. Thermostabilized chondroitinase ABC remains active at 37°C in vitro for up to 4 weeks. Chondroitin sulfate proteoglycan levels remain low in vivo up to 6 weeks post-spinal cord injury when thermostabilized chondroitin sulfate proteoglycan ABC is delivered by a hydrogel-microtube scaffold system. Axonal growth and functional recovery following the sustained local release of thermostabilized chondroitinase ABC versus a single treatment of unstabilized chondroitinase ABC demonstrate significant differences in chondroitin sulfate proteoglycan digestion. Animals treated with thermostabilized chondroitinase ABC in combination with sustained neurotrophin-3 delivery show significant improvement in locomotor function and enhanced growth of cholera toxin B subunit-positive sensory axons and sprouting of serotonergic fibers
medicine
-
intraspinal delivery of chondroitinase ABC, following T10 hemisections in adult cats, enhances adaptive movement features during a skilled locomotor task and/or promotes plasticity of spinal and supraspinal circuitry. Chondroitinase ABC enhances crossing of a peg walkway post-spinal cord injury and significantly improves ipsilateral hindlimb trajectories and integration into a functional forelimb-hindlimb coordination pattern. Recovery of these complex movements is associated with significant increases in neurofilament immunoreactivity immediately below the spinal cord injury in the ipsilateral white and contralateral gray matter. Significantly more retrogradely labeled right axotomized red nucleus neurons are seen in chondroitinase ABC-treated compared with control-treated cats indicating that a larger number of red nucleus neurons in chondroitinase ABC-treated cats had axons below the lesion level
medicine
-
role of chondroitinase ABC in the primary and secondary injury post stroke in hypertension. Renovascular hypertensive Sprague-Dawley rats underwent middle cerebral artery occlusion, and were subjected to continuous intra-infarct infusion of chondroitinase ABC for 7 days 24 h later. The intra-infarct infusion of chondroitinase ABC, by degrading accumulated chondroitin sulfate proteoglycans, rescues neuronal loss and increases the levels of growth-associated protein GAP-43 and synaptophysin in both the ipsilateral cortex and ventroposterior thalamic nucleus, indicating enhancd neuron survival as well as augmented axonal growth and synaptic plasticity, eventually improving overall neurological function
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hamai, A.; Hashimoto, N.; Mochizuki, H.; Kato, F.; Makiguchi, Y.; Horie, K.; Suzuki, S.
Two distinct chondroitin sulfate ABC lyases. An endoeliminase yielding tetrasaccharides and an exoeliminase preferentially acting on oligosaccharides
J. Biol. Chem.
272
9123-9130
1997
Proteus vulgaris
Hermel, M.; Schrage, N.F.
Efficacy of plasmin enzymes and chondroitinase ABC in creating posterior vitreous separation in the pig: a masked, placebo-controlled in vivo study
Graefes Arch. Clin. Exp. Ophthalmol.
245
399-406
2007
Proteus vulgaris
Tester, N.J.; Plaas, A.H.; Howland, D.R.
Effect of body temperature on chondroitinase ABCs ability to cleave chondroitin sulfate glycosaminoglycans
J. Neurosci. Res.
85
1110-1118
2007
Proteus vulgaris
Zhang, Z.; Park, Y.; Kemp, M.M.; Zhao, W.; Im, A.R.; Shaya, D.; Cygler, M.; Kim, Y.S.; Linhardt, R.J.
Liquid chromatography-mass spectrometry to study chondroitin lyase action pattern
Anal. Biochem.
385
57-64
2009
Pedobacter heparinus, Proteus vulgaris
Xia, Y.; Zhao, T.; Li, J.; Li, L.; Hu, R.; Hu, S.; Feng, H.; Lin, J.
Antisense vimentin cDNA combined with chondroitinase ABC reduces glial scar and cystic cavity formation following spinal cord injury in rats
Biochem. Biophys. Res. Commun.
377
562-566
2008
Proteus vulgaris
Massey, J.M.; Amps, J.; Viapiano, M.S.; Matthews, R.T.; Wagoner, M.R.; Whitaker, C.M.; Alilain, W.; Yonkof, A.L.; Khalyfa, A.; Cooper, N.G.; Silver, J.; Onifer, S.M.
Increased chondroitin sulfate proteoglycan expression in denervated brainstem targets following spinal cord injury creates a barrier to axonal regeneration overcome by chondroitinase ABC and neurotrophin-3
Exp. Neurol.
209
426-445
2008
Proteus vulgaris
Tester, N.J.; Howland, D.R.
Chondroitinase ABC improves basic and skilled locomotion in spinal cord injured cats
Exp. Neurol.
209
483-496
2008
Proteus vulgaris
Garcia-Alias, G.; Lin, R.; Akrimi, S.F.; Story, D.; Bradbury, E.J.; Fawcett, J.W.
Therapeutic time window for the application of chondroitinase ABC after spinal cord injury
Exp. Neurol.
210
331-338
2008
Proteus vulgaris
Nielsen, T.C.; Meikle, P.J.; Hopwood, J.J.; Fuller, M.
Minimum substrate requirements of endoglycosidase activities toward dermatan sulfate by electrospray ionization-tandem mass spectrometry
Glycobiology
18
1119-1128
2008
Proteus vulgaris
Laparra, J.M.; Tako, E.; Glahn, R.P.; Miller, D.D.
Isolated glycosaminoglycans from cooked haddock enhance nonheme iron uptake by Caco-2 Cells
J. Agric. Food Chem.
56
10346-10351
2008
Proteus vulgaris
Mazzoni, A.; Pashley, D.H.; Ruggeri, A.J.; Vita, F.; Falconi, M.; Di Lenarda, R.; Breschi, L.
Adhesion to chondroitinase ABC treated dentin
J. Biomed. Mater. Res. B Appl. Biomater.
86B
228-236
2008
Proteus vulgaris
Hattori, T.; Matsuyama, Y.; Sakai, Y.; Ishiguro, N.; Hirata, H.; Nakamura, R.
Chondrotinase ABC enhances axonal regeneration across nerve gaps
J. Clin. Neurosci.
15
185-191
2008
Proteus vulgaris
Lin, R.; Kwok, J.C.; Crespo, D.; Fawcett, J.W.
Chondroitinase ABC has a long-lasting effect on chondroitin sulphate glycosaminoglycan content in the injured rat brain
J. Neurochem.
104
400-408
2008
Proteus vulgaris
Cafferty, W.B.; Bradbury, E.J.; Lidierth, M.; Jones, M.; Duffy, P.J.; Pezet, S.; McMahon, S.B.
Chondroitinase ABC-mediated plasticity of spinal sensory function
J. Neurosci.
28
11998-12009
2008
Proteus vulgaris
Hrabetova, S.; Masri, D.; Tao, L.; Xiao, F.; Nicholson, C.
Calcium diffusion enhanced after cleavage of negatively charged components of brain extracellular matrix by chondroitinase ABC
J. Physiol.
587
4029-4049
2009
Proteus vulgaris
Lee, H.; McKeon, R.J.; Bellamkonda, R.V.
Sustained delivery of thermostabilized chABC enhances axonal sprouting and functional recovery after spinal cord injury
Proc. Natl. Acad. Sci. USA
107
3340-3345
2010
Proteus vulgaris
Muir, E.; Fyfe, I.; Gardiner, S.; Li, L.; Warren, P.; Fawcett, J.; Keynes, R.; Rogers, J.
Modification of N-glycosylation sites allows secretion of bacterial chondroitinase ABC from mammalian cells
J. Biotechnol.
145
103-110
2010
Proteus vulgaris
Jefferson, S.C.; Tester, N.J.; Howland, D.R.
Chondroitinase ABC promotes recovery of adaptive limb movements and enhances axonal growth caudal to a spinal hemisection
J. Neurosci.
31
5710-5720
2011
Proteus vulgaris
Klueppel, M.
Efficient secretion of biologically active chondroitinase ABC from mammalian cells in the absence of an N-terminal signal peptide
Mol. Cell. Biochem.
351
1-11
2011
Proteus vulgaris (P59807), Proteus vulgaris
Nazari-Robati, M.; Khajeh, K.; Aminian, M.; Mollania, N.; Golestani, A.
Enhancement of thermal stability of chondroitinase ABC I by site-directed mutagenesis: an insight from Ramachandran plot
Biochim. Biophys. Acta
1834
479-486
2013
Proteus vulgaris (P59807)
Chen, X.R.; Liao, S.J.; Ye, L.X.; Gong, Q.; Ding, Q.; Zeng, J.S.; Yu, J.
Neuroprotective effect of chondroitinase ABC on primary and secondary brain injury after stroke in hypertensive rats
Brain Res.
1543
324-333
2014
Proteus vulgaris
Nazari-Robati, M.; Khajeh, K.; Aminian, M.; Fathi-Roudsari, M.; Golestani, A.
Co-solvent mediated thermal stabilization of chondroitinase ABC I form Proteus vulgaris
Int. J. Biol. Macromol.
50
487-492
2012
Proteus vulgaris (P59807), Proteus vulgaris
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