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Roche

Neuraminidase (Sialidase)

from Clostridium perfringens

Synonym(s):

Sialidase

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About This Item

Enzyme Commission number:
UNSPSC Code:
12352204

biological source

bacterial (Clostridium perfringens)

Quality Level

form

lyophilized

specific activity

100 U/mg
~100 units/mg protein

mol wt

60 kDa

packaging

pkg of 5 U

manufacturer/tradename

Roche

optimum pH

5

shipped in

wet ice

storage temp.

2-8°C

General description

approximately 100 U/mg protein at +37°C and pH 5.0 with N-acetyl-neuraminosyl-D-lactose as the substrate.

Specificity

Cleaves terminal sialic-acid residues that are α2,3-, α2,6-, or α2,8-linked to Gal, GlcNAc, GalNAc, AcNeu, GlcNeu, oligosaccharides, glycolipids, or glycoproteins. Relative rate of cleavage is α2,3 >α2,8 = α2,6, determined on bonds in tri- and tetrasaccharides.

Application

Neuraminidase (Sialidase) has been used to desialylate transferrin in order to study its isoforms in human serum.
Use Neuraminidase to hydrolyze terminal N- or 0-acylneuraminic acids which are α2,3-, α2,6-, or α2,8-linked (rate α2,3: > α2,6 = α2,8) to oligosaccharides, polysaccharides, mucopolysaccharides, glycoproteins, and glycolipids.In contrast to the enzyme from Arthrobacter ureafaciens, neuraminidase from Clostridium perfringens hydrolyzes α2,3-linkages faster than α2,6-linkages. α2,8-bound sialic acids area cleaved with a similar velocity compared to α2,6-bound sialic acids.
Neuraminidase is used for:
  • Virus receptor studies
  • Studies on the interaction of lymphocytes with tumor cells
  • Cell hybridizations
  • Analysis of oligosaccharides
  • Analysis of glycoproteins
  • Analysis of glycolipids

Biochem/physiol Actions

Neuraminidase breaks α-ketosidic linkage between N-acetylneuraminic acid and the adjacent sugar residue.
Neuraminidase mediates apoptosis in the host cell before viral entry.

Preparation Note

Stabilizers: The enzyme can be stabilized by bovine serum albumin (BSA).
Storage conditions (working solution): After reconstitution in double-dist. water or sample buffer, the enzyme is stable for several weeks, stored at 2 to 8 °C; for longer storage, freezing is recommended. A stock solution may be made (e.g., at c = 5 U/100 μl). The enzyme looses approx. 50% of its activity after incubation at 37 °C for 24 hours.

Other Notes

For life science research only. Not for use in diagnostic procedures.

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

does not flash

Flash Point(C)

does not flash


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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Jitka Caslavska et al.
Journal of separation science, 40(11), 2488-2497 (2017-04-04)
Capillary electrophoresis analysis of transferrin in human serum is used to assess genetic variants after desialylation with neuraminidase and iron saturation to reduce the complexity of the transferrin pattern and thus facilitate the recognition of transferrin polymorphisms. Asialo-transferrin forms are
Ryan Septa Kurnia et al.
Veterinary world, 15(8), 1896-1905 (2022-11-01)
Clostridium toxins are widely used as medicinal agents. Many active metabolic enzymes, including sialidase (neuraminidase), hyaluronidase, and collagenase, contribute to the mechanism of action of these toxins. Sialidase from Clostridium perfringens recognizes and degrades sialic acid receptors in the host
Role of neuraminidase in influenza virus-induced apoptosis.
Morris S J, et al.
The Journal of General Virology, 80(1), 137-146 (1999)
Jesús S Aguilar Díaz de León et al.
Journal of Cancer, 12(16), 4993-5004 (2021-07-09)
Elevated concentrations of circulating low density lipoprotein (LDL) that is abnormally oxidized and desialylated is both a precursor to and a hallmark of atherosclerosis. Peripheral blood mononuclear cells (PBMCs) treated in vitro with interleukin-2 (IL-2) become lymphokine activated killer (LAK)
Analysis of genetic variants of transferrin in human serum after desialylation by capillary zone electrophoresis and capillary isoelectric focusing
Caslavska J, et al.
Journal of Separation Science, 40(11), 2488-2497 (2017)

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