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C8058

Sigma-Aldrich

Chondroitinase B from Flavobacterium heparinum

lyophilized powder (with BSA as stabilizer)

Sinónimos:

Chondroitin sulfate B lyase

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About This Item

Número de CAS:
52227-83-5
MDL number:
MFCD00166444
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

bacterial (Flavobacterium heparinum)

Quality Level

200

conjugate

(Glucosaminoglycan)

form

lyophilized powder (with BSA as stabilizer)

shipped in

dry ice

storage temp.

−20°C

Categorías relacionadas

Application

Chondroitinase B from Flavobacterium heparinum has been used in a study to assess the structural characterization and antithrombin activity of dermatan sulfate. Chondroitinase B from Flavobacterium heparinum has also been used in a study to investigate the chondroitin lyase action pattern via liquid chromatography–mass spectrometry.
The enzyme from Sigma has been used for the analysis of the frequency of iduronic acid in dermatan sulfate dodecasaccharide. It has also been used to digest dermatan sufate (DS) in melanoma cells. This digestion resulted in decreased proliferation and invasiveness of tumor cells, thereby suggesting a role for DS in metastasis.

Biochem/physiol Actions

Chondroitinase B degrades only chondroitin sulphate B producing oligo- and tetra-saccharides, and an unsaturated 4-sulphated disaccharide. It has an optimum temperature of 20 °C and an optimum pH of 8.0. The enzyme activity is inhibited by 50% using 0.1 M NaCI. Co2+, Fe3+ and Ba2+ also inhibit its activity.

Unit Definition

One unit will form 0.1 μmole of unsaturated uronic acid per hr at pH 7.5 at 25°C using chondroitin sulfate B as substrate.

pictograms

Exclamation mark
GHS07

signalword

Warning

hcodes

H319

Hazard Classifications

Eye Irrit. 2

Storage Class

13 - Non 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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Zhenqing Zhang et al.
Analytical biochemistry, 385(1), 57-64 (2008-11-11)
Liquid chromatography-mass spectrometry was applied to determine the action pattern of different chondroitin lyases. Two commercial enzymes, chondroitinase ABC (Proteus vulgaris) and chondroitinase ACII (Arthrobacter aurescens), having action patterns previously determined by viscosimetry and gel electrophoresis were first examined. Next
Y M Michelacci et al.
The Biochemical journal, 151(1), 121-129 (1975-10-01)
A chondroitinase that degrades only chondroitin sulphate B was isolated from Flavobacterium heparinum, and separated from a constitutive chondroitinase AC also present in extracts of F. heparinum. The enzyme acts only on chondroitin sulphate B, producing oligo- and tetra-saccharides, plus
Yvette M Coulson-Thomas et al.
Journal of neuroscience methods, 171(1), 19-29 (2008-04-18)
Injury to the CNS of vertebrates leads to the formation of a glial scar and production of inhibitory molecules, including chondroitin sulphate proteoglycans. Various studies suggest that the sugar component of the proteoglycan is responsible for the inhibitory role of
Gerdy B ten Dam et al.
The American journal of pathology, 171(4), 1324-1333 (2007-08-25)
Chondroitin sulfate (CS) is abundantly present in the tumor stroma, and tumor-specific CS modifications might be potential targets to influence tumor development. We applied the phage display technology to select antibodies that identify these tumor-specific CS modifications. Antibody GD3G7 was
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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