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G4259

Sigma-Aldrich

β-Glucuronidase from Helix aspersa (garden snail)

Type HA-4

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About This Item

Enzyme Commission number:
3.2.1.31 (BRENDA, IUBMB)
EC Number:
232-606-8
MDL number:
MFCD00130629
UNSPSC Code:
12352204
NACRES:
NA.54

type

Type HA-4

Quality Level

200

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

pictograms

Health hazard
GHS08

signalword

Danger

Hazard Classifications

Resp. Sens. 1 - Skin Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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β-Glucuronidase from Escherichia coli Type VII-A, lyophilized powder, 5,000,000-20,000,000 units/g protein, pH 6.8 (30 min assay)

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β-Glucuronidase from Escherichia coli

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)
Catalytic mechanisms of enymatic glycosyl transfer
M.L. Sinnott
Chemical Reviews, 90, 1171-1202 (1990)
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
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
View All Related Papers

Protocols

Using UHPLC/MS (TOF) for Detection of Drugs and Metabolites in Urine Following Optimized Enzymatic Hydrolysis Conditions

To optimize hydrolysis using β-glucuronidase, factors such as incubation time, temperature, hydrolysis pH, enzyme source, and enzyme concentration must be evaluated for each glucuronide metabolite to be analyzed.

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