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N5631

Sigma-Aldrich

Neuraminidase from Clostridium perfringens (C. welchii)

Type VIII, lyophilized powder, 10-20 units/mg protein (using 4MU-NANA), 3.5-8.0 units/mg protein (mucin)

Synonym(s):

Acyl-neuraminyl Hydrolase, Receptor-destroying enzyme, Sialidase

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About This Item

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

type

Type VIII

Quality Level

form

lyophilized powder

specific activity

10-20 units/mg protein (using 4MU-NANA)
3.5-8.0 units/mg protein (mucin)

composition

Protein, ≥85% biuret

foreign activity

Protease and NAN-aldolase, present

storage temp.

−20°C

Gene Information

Clostridium perfringens str. 13 ... nanI(988807)

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General description

Neuraminidase enzymes are glycoside hydrolase enzymes that catalyze hydrolysis of terminal sialic acid residues. The most well-known are the viral nearamidases, which promote influenza virus release.

Application

Neuraminidase from Clostridium perfringens has been used in a study to assess the binding characteristics of iota toxin by fluorescence-activated cytometry. It has also been used in a study to investigate the distribution of neuraminidase among food poisoning strains.

Biochem/physiol Actions

Neuraminidase cleavage of sialic acid groups has been used to study recognition by antibodies of glycoprotein structures. The use of neuraminidase in the estimation of N-acetylneuraminic acid was compared favorably to two other methods.
Neuraminidases are used to cleave terminal N-acetyl neuraminic acid (sialic acid) from a variety of glycoproteins. The enzyme from Clostridium perfringens cleaves terminal sialic acid residues which are α-2,3- α-2,6- or α-2,8-linked to Gal, GlcNac, GalNAc, AcNeu, GlcNeu, oligosaccharides, glycolipids or glycoproteins. The relative rate of cleavage decreases in the order: α-2-3 > α-2-6 . α-2-8. Neuraminidase from C. perfringens cleaves α-2-3 linked sialic acid residues most efficiently, compared to A. ureafaciens, (Sigma N3642) which preferentially cleaves α-2-6 linked residues.
The degradation of gangliosides grown in lipid mono layers by Clostridium perfringens neuraminidase depends largely on surface pressure. Increased pressure can inhibit neuraminidase activity.
The use of neuraminidase to remove sialic acid residues from glycoproteins on cell surfaces has been frequently reported. Generally, procedures have indicated using neuraminidase in PBS at 37°C for 30 minutes, followed by several washings with PBS. Treatment of tissue sections with neuraminidase at much lower concentrations require longer incubation: for 1-4 U/mL in 0.1 M acetate buffer pH 4.2-5, from 2 to 20 hours at 37 °C.

Unit Definition

One unit will liberate 1.0 micromole of N-acetyl neuraminic acid per minute at pH 5.0 at 37 °C using bovine submaxillary mucin.

One unit will hydrolyze 1.0 micromole of 2′-(4-methylumbelliferyl)-a-D-N-actetylneuraminic acid per minute at pH 5.0 at 37 °C (using 4MU-NANA as a substrate)

Preparation Note

Chromatographically purified from Type V (N 2876)

Analysis Note

Package sizes based on 4MU-NANA units
Package sizes based on the 4MU-NANA units

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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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B G Stiles et al.
Infection and immunity, 68(6), 3475-3484 (2000-05-19)
The binding characteristics of iota toxin, a binary enterotoxin produced by Clostridium perfringens type E, were studied by fluorescence-activated cytometry. The proteolytically activated binding component of iota toxin, iota b (Ib), bound to various cell types when incubated at 4
M A Perillo et al.
Biochimica et biophysica acta, 1193(1), 155-164 (1994-07-13)
The activity of Clostridium perfringens neuraminidase against gangliosides GM3, GD1a and GM1 was studied in lipid monolayers at the air-buffer solution interface. The enzyme activity assay against pure ganglioside monolayers is based on the markedly different molecular packing areas of
Distribution of Neuraminidase among Food-poisoning Strains of Clostridium perfringens
Moss, C.
Applied and Environmental Microbiology, 15, 718-722 (1967)
Gangliosides: structure, isolation, and analysis.
R W Ledeen et al.
Methods in enzymology, 83, 139-191 (1982-01-01)
A simple method for the purification of commercial neuraminidase preparations free from proteases.
M W Hatton et al.
Biochimica et biophysica acta, 327(1), 114-120 (1973-11-15)

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