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SRE0023

Sigma-Aldrich

β-Glucuronidase from abalone

Purified, aqueous solution, β-glucuronidase 150,000-250,000 units/mL, β-glucuronidase ≥20,000,000 units/g protein

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About This Item

Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

Quality Level

form

aqueous solution

β-glucuronidase activity

≥20,000,000 units/g protein
150,000-250,000 units/mL

secondary activity

≤7,500 units/mL sulfatase

storage temp.

2-8°C

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Related Categories

Application

Technical Article Comparing Performance of Different Enzymes
Learn more
about recent application data generated by Sigma R&D to optimize hydrolysis for different drug classes using enzymes from different sources and the use of a chromatographicaly purified enzyme to reduce the effect of esterase activity resulting in conversion of 6-MAM to Morphine.

Biochem/physiol Actions

β-Glucuronidase (GUSB) is a lysosomal enzyme, that degrades glucuronate-containing glycosaminoglycans. β-glucuronidase, obtained from abalone has the ability to hydrolyze samples, that has high analyte concentrations. Absence of β-glucuronidase results in mucopolysaccharidosis type VII (MPSVII), which leads to lysosomal storage in the brain.

Unit Definition

One Sigma or modified Fishman unit will liberate 1.0 μg of phenolphthalein from phenolphthalein glucuronide per hr at 37 °C at pH 3.8 (30 min assay).

Physical form

Supplied as an aqueous solution containing L-proline, ammonium acetate and sodium azide

Storage Class Code

10 - Combustible liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Evaluation of abalone beta-glucuronidase substitution in current urine hydrolysis procedures
Malik W B, et al.
Journal of Analytical Toxicology, 38(3), 171-176 (2014)
Human beta-glucuronidase: structure, function, and application in enzyme replacement therapy
Naz H, et al.
Rejuvenation Research, 16(5), 352-363 (2013)

Articles

β-glucuronidase (GUS) enzymes are utilized to hydrolyze glucuronide (gluc) drug metabolites to the parent drug, facilitating analysis by LC-MS/MS.

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