G4259
β-Glucuronidase from Helix aspersa (garden snail)
Type HA-4
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About This Item
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-606-8
MDL number:
Product Name
β-Glucuronidase from Helix aspersa (garden snail), Type HA-4
type
Type HA-4
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
Quality Level
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.
Other Notes
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.
Used for the hydrolysis of glucuronide conjugates in urinary metabolite analysis
signalword
Danger
hcodes
Hazard Classifications
Resp. Sens. 1 - Skin Sens. 1
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Vectors with the gus reporter gene for identifying and quantitating promoter regions in <I>Saccharomyces cerevisiae</I>
Marathe & J.E. McEwen
Gene, 154, 105-107 (1988)
Catalytic mechanisms of enymatic glycosyl transfer
M.L. Sinnott
Chemical Reviews, 90, 1171-1202 (1990)
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
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
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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