ACETYLNEURAMINYL HYDROLASE

Base Information

• Chemical Name: ACETYLNEURAMINYL HYDROLASE
• CAS No.: 9001-67-6
• Molecular Formula: NULL
• Molecular Weight: 0
• Mol file: 9001-67-6.mol

Synonyms:ALPSeparator;Acetylneuraminidase;Arylneuraminidase;E.C. 3.2.1.18;Exo-a-sialidase;N-Acetylneuraminidase;N-Acylneuraminyl hydrolase;Parasite-derived mimic ofneurotrophic factors;Sialidase;a-Neuraminidase;

Chemical Property of ACETYLNEURAMINYL HYDROLASE

Chemical Property:

• Appearance/Colour: white liquid /solid
• PSA: 0.00000
• Density: 1.00 g/mL at 20 °C
• LogP: 0.00000
• Storage Temp.: 2-8°C
• Water Solubility.: Soluble in water or 10mM phosphate buffer, pH 6.0

Purity/Quality:

98%,99%, ^*data from raw suppliers

Neuraminidase ^*data from reagent suppliers

Safty Information:

• Safety Statements: 22-24/25

MSDS Files:

SDS file from LookChem

Total 1 MSDS from other Authors

Useful:

• Uses: Neuraminidase is used as a hydrolytic enzyme that removes sialic acid from mucoproteins, used in a study to assess binding with human T lymphocytes in sheep pretreated with neuraminidase. It has also been used in a study to investigate the effect of bile salts on the action of hydrolysis by neuraminidase. Neuraminidase is an important deglycosylation enzyme capable of cleaving all non-reducing unbranched N-acetylneuraminic and N-glycolylneuraminic acid residues by hydrolysis of α(2→6), α(2→3), α(2→8), and α(2→9) linkages (affinity in the order given). Branched sialic acids may also be cleaved with the use of high concentrations of enzyme and prolonged incubations. Desialylated glycoproteins may then be further characterized by treatment with various exoglycosidases resulting in partial or complete O-deglycosylation. SDS-PAGE and MALDI-TOF MS are typically utilized in purification, structural analysis, and sequencing process. These techniques also remove heterogeneity and charge from the glycoprotein. Neuraminidase from Vibrio cholera has been used in a study to describe a five-step purification method. It has also been used in a study to investigate modification of leukemia L1210 tumor cells.