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Merck

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:
MFCD00130629
EC Number:
3.2.1.31 (BRENDA, IUBMB)
Specific activity:
≥300,000 units/g solid solid

Key Documents

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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

200

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

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H334

Storage Class

11 - Combustible Solids

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Hazard Classifications

Resp. Sens. 1

wgk

WGK 1

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Certificates of Analysis (COA)

Lot/Batch Number
098K37941
098K3794
017K3785
117H3896
100K3784

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Vectors with the gus reporter gene for identifying and quantitating promoter regions in <I>Saccharomyces cerevisiae</I>
Marathe &amp; J.E. McEwen
Gene, 154, 105-107 (1988)
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
M.L. Sinnott
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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Protocols

UHPLC/MS for Drug Detection in Urine

Optimize β-glucuronidase hydrolysis for glucuronide metabolite analysis considering factors like time, temperature, pH, and enzyme concentration.

ß-Glucuronidase Enzymatic Assay

Enzymatic assay protocol for β-Glucuronidase from Helix Pomatia and Bovine Liver aids laboratory personnel in following procedures.

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