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G4259

Sigma-Aldrich

β-Glucuronidase from Helix aspersa (garden snail)

Type HA-4

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About This Item

Número da licença da enzima:
3.2.1.31 (BRENDA, IUBMB)
Número CE:
232-606-8
Número MDL:
MFCD00130629
Código UNSPSC:
12352204
NACRES:
NA.54

tipo

Type HA-4

forma

partially purified powder

atividade específica

≥300,000 units/g solid solid

secondary activity

≤7,500 units/g solid sulfatase

solubilidade

H2O: soluble 1.90-2.10 mg/mL, clear to slightly hazy

aplicação(ões)

clinical testing

temperatura de armazenamento

−20°C

Categorias relacionadas

Aplicação

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.

Ações bioquímicas/fisiológicas

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.

Definição da unidade

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.

Outras notas

Used for the hydrolysis of glucuronide conjugates in urinary metabolite analysis

Pictogramas

Health hazard
GHS08

Palavra indicadora

Danger

Frases de perigo

H317,H334

Declarações de precaução

P261 - P280 - P342 + P311

Classificações de perigo

Resp. Sens. 1 - Skin Sens. 1

Código de classe de armazenamento

11 - Combustible Solids

Classe de risco de água (WGK)

WGK 3

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

Equipamento de proteção individual

Eyeshields, Gloves, type N95 (US)

Certificados de análise (COA)

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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)
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
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Protocolos

Enzymatic Assay of ß-Glucuronidase (EC 3.2.1.31) from Helix Pomatia and Bovine Liver

Enzymatic Assay of ß-Glucuronidase (EC 3.2.1.31) from Helix Pomatia and Bovine Liver

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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