N5631
Neuraminidase from Clostridium perfringens (C. welchii)
Type VIII, lyophilized powder, 10-20 units/mg protein (using 4MU-NANA), 3.5-8.0 units/mg protein (mucin)
Sinónimos:
Acyl-neuraminyl Hydrolase, Receptor-destroying enzyme, Sialidase
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About This Item
Productos recomendados
tpo
Type VIII
Nivel de calidad
formulario
lyophilized powder
actividad específica
10-20 units/mg protein (using 4MU-NANA)
3.5-8.0 units/mg protein (mucin)
composición
Protein, ≥85% biuret
actividad extraña
Protease and NAN-aldolase, present
temp. de almacenamiento
−20°C
Información sobre el gen
Clostridium perfringens str. 13 ... nanI(988807)
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Descripción general
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.
Aplicación
Neuraminidase from Clostridium perfringens has been used in a study to assess the binding characteristics of iota toxin by fluorescence-activated cytometry. It has also been used in a study to investigate the distribution of neuraminidase among food poisoning strains.
Acciones bioquímicas o fisiológicas
Neuraminidase cleavage of sialic acid groups has been used to study recognition by antibodies of glycoprotein structures. The use of neuraminidase in the estimation of N-acetylneuraminic acid was compared favorably to two other methods.
Neuraminidases are used to cleave terminal N-acetyl neuraminic acid (sialic acid) from a variety of glycoproteins. The enzyme from Clostridium perfringens cleaves terminal sialic acid residues which are α-2,3- α-2,6- or α-2,8-linked to Gal, GlcNac, GalNAc, AcNeu, GlcNeu, oligosaccharides, glycolipids or glycoproteins. The relative rate of cleavage decreases in the order: α-2-3 > α-2-6 . α-2-8. Neuraminidase from C. perfringens cleaves α-2-3 linked sialic acid residues most efficiently, compared to A. ureafaciens, (Sigma N3642) which preferentially cleaves α-2-6 linked residues.
The degradation of gangliosides grown in lipid mono layers by Clostridium perfringens neuraminidase depends largely on surface pressure. Increased pressure can inhibit neuraminidase activity.
The use of neuraminidase to remove sialic acid residues from glycoproteins on cell surfaces has been frequently reported. Generally, procedures have indicated using neuraminidase in PBS at 37°C for 30 minutes, followed by several washings with PBS. Treatment of tissue sections with neuraminidase at much lower concentrations require longer incubation: for 1-4 U/mL in 0.1 M acetate buffer pH 4.2-5, from 2 to 20 hours at 37 °C.
Definición de unidad
One unit will liberate 1.0 micromole of N-acetyl neuraminic acid per minute at pH 5.0 at 37 °C using bovine submaxillary mucin.
One unit will hydrolyze 1.0 micromole of 2′-(4-methylumbelliferyl)-a-D-N-actetylneuraminic acid per minute at pH 5.0 at 37 °C (using 4MU-NANA as a substrate)
One unit will hydrolyze 1.0 micromole of 2′-(4-methylumbelliferyl)-a-D-N-actetylneuraminic acid per minute at pH 5.0 at 37 °C (using 4MU-NANA as a substrate)
Nota de preparación
Chromatographically purified from Type V (N 2876)
Nota de análisis
Package sizes based on 4MU-NANA units
Package sizes based on the 4MU-NANA units
Palabra de señalización
Danger
Frases de peligro
Consejos de prudencia
Clasificaciones de peligro
Resp. Sens. 1
Código de clase de almacenamiento
11 - Combustible Solids
Clase de riesgo para el agua (WGK)
WGK 1
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
Equipo de protección personal
Eyeshields, Gloves, type N95 (US)
Certificados de análisis (COA)
Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»
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Los clientes también vieron
B G Stiles et al.
Infection and immunity, 68(6), 3475-3484 (2000-05-19)
The binding characteristics of iota toxin, a binary enterotoxin produced by Clostridium perfringens type E, were studied by fluorescence-activated cytometry. The proteolytically activated binding component of iota toxin, iota b (Ib), bound to various cell types when incubated at 4
M A Perillo et al.
Biochimica et biophysica acta, 1193(1), 155-164 (1994-07-13)
The activity of Clostridium perfringens neuraminidase against gangliosides GM3, GD1a and GM1 was studied in lipid monolayers at the air-buffer solution interface. The enzyme activity assay against pure ganglioside monolayers is based on the markedly different molecular packing areas of
Distribution of Neuraminidase among Food-poisoning Strains of Clostridium perfringens
Moss, C.
Applied and Environmental Microbiology, 15, 718-722 (1967)
Gangliosides: structure, isolation, and analysis.
R W Ledeen et al.
Methods in enzymology, 83, 139-191 (1982-01-01)
A simple method for the purification of commercial neuraminidase preparations free from proteases.
M W Hatton et al.
Biochimica et biophysica acta, 327(1), 114-120 (1973-11-15)
Protocolos
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