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MilliporeSigma

G4259

β-Glucuronidase from Helix aspersa (garden snail)

Type HA-4

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A propos de cet article

UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-606-8
MDL number:
Numéro CE :
Specific activity:
≥300,000 units/g solid solid
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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

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

signalword

Danger

Classe de stockage

11 - Combustible Solids

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

hcodes

Hazard Classifications

Resp. Sens. 1

wgk

WGK 1



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Protocoles

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

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


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



Numéro d'article de commerce international

RéférenceGTIN
G4259-1MU04061833630679