A2264
β-N-Acetylglucosaminidase from Canavalia ensiformis (Jack bean)
ammonium sulfate suspension, ≥8 units/mg protein
Synonym(s):
β-N-Acetyl-D-hexosaminide N-acetylhexosaminohydrolase, β-N-Acetylhexosaminidase
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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-730-2
MDL number:
Specific activity:
≥8 units/mg protein
Biological source:
Canavalia ensiformis
biological source
Canavalia ensiformis
form
ammonium sulfate suspension
foreign activity
α- and β-galactosidase, and α-L-fucosidase ≤0.1%, α-mannosidase ≤0.5%
storage temp.
2-8°C
Quality Level
specific activity
≥8 units/mg protein
Related Categories
Application
β -N-acetylglucosaminidase is a lysosomal enzyme used to hydrolyze N-acetyl-β-D-glucosaminides and N-acetyl-β-Dgalactosaminides. It is used in chemoenzymatic synthesis of oligosaccharides based on their effective transglycosylation of β-GlcNAc and β-GalNAcc. It may be a useful tool to study Alzheimer′s Disease . Acetylglucosaminidase from Canavalia ensiformis has been used to study enzymic detachment of biofilms .
Biochem/physiol Actions
This enzyme, sometimes called β-N-acetylhexosaminidase, is reported to liberate terminal β-linked N-acetylglucosamine and N-acetylgalactosamine from a variety of substrates.
This enzyme, sometimes called β-N-acetylhexosaminidase, is reported to liberate terminal β-linked N-acetylglucosamine and N-acetylgalactosamine from a variety of substrates. The activity of β-N-actylglucosaminidase may be determined with the chromogenic substrate p-nitrophenyl-N-acetyl-β-D-glucosaminide. β-N-actylglucosaminidase hydrolyzes the terminal nonreducing N-acetyl-D-hexosamine residues. This enzyme contains two predominant isozymes, Hex A, a heterodimer, and Hex B, a homodimer. N-acetylglucosamine, acetamide, N-2-acetamido-2-deoyglucosylamine, N-acetylnojirimycin, and N-acetyldeoxynojirmycin are known inhibitors.
Physical form
Suspension in 2.5 M (NH4)2SO4, pH 7.0
Analysis Note
At pH 4.0, p-nitrophenyl β-N-acetylgalactosaminide is hydrolyzed at approximately 50% of the rate of hydrolysis of p-nitrophenyl β-N-acetylglucosaminide at pH 5.0.
Other Notes
One unit will hydrolyze 1.0 μmole of p-nitrophenyl N-acetyl-β-D-glucosaminide to p-nitrophenol and N-acetyl-D-glucosamine per min at pH 5.0 at 25 °C.
flash_point_f
Not applicable
flash_point_c
Not applicable
Storage Class
10 - Combustible liquids
Regulatory Information
低风险生物材料
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Mohammed A Al-Fattani et al.
Journal of medical microbiology, 55(Pt 8), 999-1008 (2006-07-20)
Matrix material was extracted from biofilms of Candida albicans and Candida tropicalis and analysed chemically. Both preparations contained carbohydrate, protein, hexosamine, phosphorus and uronic acid. However, the major component in C. albicans matrix was glucose (32%), whereas in C. tropicalis
T Berger et al.
Journal of reproduction and fertility, 86(2), 559-565 (1989-07-01)
An assay to determine the binding of pig spermatozoa to the zona pellucida (ZP) of pig oocytes was developed using conditions compatible with in-vitro fertilization of pig eggs and with pig sperm penetration of zona-free hamster ova. These conditions were
Chaeyoung Kim et al.
Neurobiology of aging, 34(1), 275-285 (2012-04-17)
Deposition of β-amyloid (Aβ) as senile plaques and disrupted glucose metabolism are two main characteristics of Alzheimer's disease (AD). It is unknown, however, how these two processes are related in AD. Here we examined the relationship between O-GlcNAcylation, which is
Tyler Mark Pierson et al.
Molecular genetics and metabolism, 108(1), 65-69 (2012-11-20)
A 12 year-old female presented with a seven-year history of progressive muscle weakness, atrophy, tremor and fasciculations. Cognition was normal. Rectal biopsy revealed intracellular storage material and biochemical testing indicated low hexosaminidase activity consistent with juvenile-onset G(M2)-gangliosidosis. Genetic evaluation revealed
David J Vocadlo
Current opinion in chemical biology, 16(5-6), 488-497 (2012-11-14)
The addition of N-acetylglucosamine (GlcNAc) O-linked to serine and threonine residues of proteins is known as O-GlcNAc. This post-translational modification is found within multicellular eukaryotes on hundreds of nuclear and cytoplasmic proteins. O-GlcNAc transferase (OGT) installs O-GlcNAc onto target proteins
Articles
Instructions for working with enzymes supplied as ammonium sulfate suspensions
以硫酸铵悬浮液形式提供的酶的使用指南
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