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N5254

Sigma-Aldrich

Neuraminidase Agarose from Clostridium perfringens (C. welchii)

Type VI-A, ammonium sulfate suspension

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Synonym(s):
Acylneuraminyl hydrolase, Receptor-destroying enzyme, Sialidase
Enzyme Commission number:
MDL number:
NACRES:
NA.54

type

Type VI-A

Quality Level

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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This Item
N5521N2133N5631
Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

200

form

ammonium sulfate suspension

form

buffered aqueous solution

form

lyophilized powder

form

lyophilized powder

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

−20°C

type

Type VI-A

type

-

type

Type X

type

Type VIII

extent of labeling

0.6-1.8 units per mL gel

extent of labeling

-

extent of labeling

-

extent of labeling

-

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).

Storage Class

6.2 - Infectious substances

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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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
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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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