N5254
Neuraminidase Agarose from Clostridium perfringens (C. welchii)
Type VI-A, ammonium sulfate suspension
Synonyme(s) :
Acylneuraminyl hydrolase, Receptor-destroying enzyme, Sialidase
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A propos de cet article
Specific activity:
20-60 units/g agarose
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Type VI-A
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
Quality Level
Catégories apparentées
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.
Physical form
Suspension in 2.0 M (NH4)2SO4 solution, pH 7.0.
Preparation Note
Prepared from Neuraminidase, Type VI (N 3001).
Other Notes
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.
Classe de stockage
12 - Non Combustible Liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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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
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
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
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)
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