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You are here:Home » Molecular Biology » MB-Enzymes, Glycosidase » Neuraminidase, Clostridium perfringens

Neuraminidase, Clostridium perfringens


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Neuraminidase (sialidase) splits off N-acetyl neuraminic acid (sialic acid) from a variety of glycoproteins and are important tools for the study of glycoproteins in protein chemistry and cell biology (Hatton et al. 1973). Chromatographic purification has been developed in this laboratory based on work of Cassidy et al. (1965). Wooley and Gommi (1966) describe the use of this neuraminidase in a method for measuring serotonin receptors. It is also employed to determine bound N-acetylneuraminic acid in tissues. Considerable interest has been shown in using neuraminidase inhibitors as possible anti-viral and anti-bacterial agents.
Catalog #N2100
Protein Content (%) 30%
Units/Protein (u/mg) 10u/mg Protein
Assay Method The assay is based on the measurement of sialic acid (NANA) released from bovine submaxillary mucin. One unit causes the release of one micromole of sialic acid per minute at 37°C and pH 5.0, from bovine submaxillary mucin under the specified conditions.
SourceCI. perfringens
PuritySupplied as a lyophilized powder, 50% sucrose.
Concentration~20u/mg (dry weight)
Important NoteThis product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.
Alternate namesEC=; Clostridium perfringens

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