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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:
MDL number:
UNSPSC Code:
12352204
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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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_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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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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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