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N5254

Sigma-Aldrich

Neuraminidase Agarose from Clostridium perfringens (C. welchii)

Type VI-A, ammonium sulfate suspension

Synonym(s):

Acylneuraminyl hydrolase, Receptor-destroying enzyme, Sialidase

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About This Item

Enzyme Commission number:
3.2.1.18 (BRENDA, IUBMB)
MDL number:
MFCD00131711
UNSPSC Code:
12352204
NACRES:
NA.54

type

Type VI-A

Quality Level

200

form

ammonium sulfate suspension

specific activity

20-60 units/g agarose

extent of labeling

0.6-1.8 units per mL gel
20-60 units per g agarose

matrix

beaded agarose

storage temp.

2-8°C

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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

Agarose-linked neuraminidase from Clostridium perfringens can be used for the detection of total and desialylated sex hormone-binding globulin in human serum samples.
Neuraminidase from Clostridium perfringens has been used in a study to assess a genetic polymorphism of human serum glycoprotein (inter-α-trypsin-inhibitor). It has also been used in a study to investigate the inhibition of neuraminidase by chemically sulphated glycopeptides.

Unit Definition

One unit will liberate 1.0 μmole of N-acetylneuraminic acid per min at pH 5.0 at 37 °C using NAN-lactose or bovine submaxillary mucin, unless otherwise specified. Prices based on units using NAN-lactose as substrate.

Physical form

Suspension in 2.0 M (NH4)2SO4 solution, pH 7.0.

Preparation Note

Prepared from Neuraminidase, Type VI (N 3001).

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

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T I Arnon et al.
European journal of immunology, 31(9), 2680-2689 (2001-09-06)
Natural killer (NK) cells destroy virus-infected and tumor cells without prior antigen stimulation. The NK cell cytotoxicity is regulated in large part by the expression of NK cell receptors that are able to bind major histocompatibility complex (MHC) class I
N Mian et al.
The Biochemical journal, 181(2), 377-385 (1979-08-01)
Chemically sulphated glycopeptides (derived from pig duodenal mucosa) inhibited Clostridium perfringens neuraminidase (EC 3.2.1.18) activity in a pH-dependent manner. Analysis of inhibition kinetics data indicated that, although the enzyme inhibition could not be categorized into any of the classical types
The mechanisms controlling the recognition of tumor- and virus-infected cells by NKp46
Arnon, T.I., et al
Immunobiol., 103(2), 664-672 (2004)
Measurements of total and desialylated sex hormone binding globulin in serum by ELISA.
J Vaysse et al.
Clinical chemistry, 44(4), 882-884 (1998-04-29)
U Vogt et al.
Human genetics, 84(2), 151-154 (1990-01-01)
A new genetic polymorphism of a human serum glycoprotein, the inter-alpha-trypsin-inhibitor (ITI), has been demonstrated by population and family studies. Sera were examined after neuraminidase treatment by isoelectric focusing on agarose gels followed by immunoblotting or by immunofixation with specific
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