G4259
β-Glucuronidase from Helix aspersa (garden snail)
Type HA-4
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About This Item
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
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type
Type HA-4
Quality Level
form
partially purified powder
specific activity
≥300,000 units/g solid solid
secondary activity
≤7,500 units/g solid sulfatase
solubility
H2O: soluble 1.90-2.10 mg/mL, clear to slightly hazy
application(s)
clinical testing
storage temp.
−20°C
Related Categories
Application
β-glucuronidase was used in enzymic hydrolysis of tissue homogenates for liquid chromatography-electrospray ion trap mass spectrometry (LC/MSn) analysis, to study the structures of degradation products of baicalin.
Biochem/physiol Actions
β-glucuronidase (β-GIc) is an exoglycosidase that catalyzes the breakdown of complex carbohydrates. In humans it converts conjugated bilirubin into the unconjugated form, making bilirubin suitable for reabsorption.
Unit Definition
One Sigma or modified Fishman unit will liberate 1.0 μg of phenolphthalein from phenolphthalein glucuronide per hr at 37°C at the pH 5.0 (30 min assay).
One unit of sulfatase will hydrolyze 1.0 μmole p-nitrocatechol sulfate per hr at pH 5.0 at 37 °C.
Other Notes
Used for the hydrolysis of glucuronide conjugates in urinary metabolite analysis
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1 - Skin Sens. 1
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)
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J D McCarter et al.
Current opinion in structural biology, 4(6), 885-892 (1994-12-01)
The determination of a large number of three-dimensional structures of glycosidases, both free and in complex with ligands, has provided valuable new insights into glycosidase catalysis, especially when coupled with results from studies of specifically labelled glycosidases and kinetic analyses
S Jain et al.
Nature structural biology, 3(4), 375-381 (1996-04-01)
The X-ray structure of the homotetrameric lysosomal acid hydrolase, human beta-glucuronidase (332,000 Mr), has been determined at 2.6 A resolution. The tetramer has approximate dihedral symmetry and each promoter consists of three structural domains with topologies similar to a jelly
Catalytic mechanisms of enymatic glycosyl transfer
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Chemical Reviews, 90, 1171-1202 (1990)
Jie Xing et al.
Journal of pharmaceutical and biomedical analysis, 39(3-4), 593-600 (2005-05-17)
The stability of baicalin in buffered aqueous solutions at different pHs and in biological fluids, including plasma, urine and tissue homogenates, were investigated in vitro. Structures of the degradation products of baicalin were elucidated by liquid chromatography-electrospray ion trap mass
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