H2N2V1, France, Analysis, bibRecord, 000318

Neuraminidase from influenza virus A (H3N2). Specificity towards several substrates and procedure of activity determination

Identifieur interne : 000318 ( France/Analysis ); précédent : 000317; suivant : 000319

Neuraminidase from influenza virus A (H3N2). Specificity towards several substrates and procedure of activity determination

Auteurs : Jose A. Cabezas [Espagne] ; Pedro Calvo [Espagne] ; Pierre Eid [France] ; Josefa Martin [Espagne] ; Nieves Perez [Espagne] ; Angel Reglero [Espagne] ; Claude Hannoun [France]

Source :

BBA - Enzymology [ 0005-2744 ] ; 1980.

RBID : ISTEX:0A3CF38109D98BA00CD3F6B2B1B6FFE1D3347B2C

English descriptors

Teeft :
- Academic press, Acta, Acta chem, Acylneuraminyl hydrolase, Assay, Assay conditions, Biochem, Biophys, Bovine serum albumin, Bovine submaxillary mucin, Chem, Colominic acid, Colored quinone, Different types, English edition, Enzyme activity, Fetuin, First peak, Glycoprotein, Glycosyl transferase activity, Gottschalk, Horse brain, Influenza, Influenza virus, Institut pasteur, Methods enzymol, Molar extinction coefficient, Molecular weight, Mucin, Nadh, Nadh procedure, Natural substrates, Neuraminidase, Neuraminidase activity, Neuraminidase activity determination, Neuraminidases, Other hand, Other methods, Porcine submaxillary mucin, Potassium phosphate buffer, Purification procedure, Same buffer, Schauer, Several substrates, Sialic, Sialic acid, Sialic acids, Simple procedure, Submaxillary, Vaccine, Verlag chemie, Virus neuraminidases.

Abstract

Abstract: Neuraminidase (acelneuraminyl hydrolase, EC 3.2.1.18) from the influenza virus A/Hong Kong/68 (H3N2) was purified after treatment of the purified virus with sarcosyl (sodium laurylsarcosinate) centrifugation at 110 000 × g, and chromatography on DEAE-Sephadex and Sephadex G-200. It migrated as a single component during electrophoresis on polyacrylamide gel, and its molecular weight was estimated about 270 000.The enzyme was thermolabile, the activity being reduced to 60% in 10 min at 50°C. The purified neuraminidase had an apparent Km value of 4.1 · 10−3 M for 5-N-acetyl-2-O-(3-methoxyphenyl)-α-d-neuraminic acid and was able to release sialic acid with linkages α2–3, α2–6 and α2–8 (with very different efficiency) from fetuin, gangliosides, colominic acid, and bovine and porcine submaxillary mucines.The enzymic activity was measured by several procedures: (A) spectrophotometric determination at 340 nm of the NADH produced in the reaction catalysed by β-galactose dehydrogenase on β-galactose + NAD+, this β-galactose was the product released from lactose by β-galactosidase and lactose was the product of the neuraminidase activity on N-acetylneuraminyl-lactose; (B) determination of the colored quinone yielded by the liberated methoxyphenol with 4-aminoantipyrine (Santer, U.V., Yee-Foon, J. and Glick, M.C. (1978) Biochim. Biophys. Acta 523, 435–442); (C) periodate-thiobarbiturate procedures (Warren, L. (1959) J. Biol. Chem. 234, 1971–1975 or Aminoff, D. (1961) Biochem. J. 81, 384–391). Some peculiarities of these methods are discussed.

Url:

https://api.istex.fr/ark:/67375/6H6-DBPKV5RT-W/fulltext.pdf

DOI: 10.1016/0005-2744(80)90141-2

Affiliations:

Espagne, France

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ISTEX:0A3CF38109D98BA00CD3F6B2B1B6FFE1D3347B2C

Le document en format XML

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<front><div type="abstract" xml:lang="en">Abstract: Neuraminidase (acelneuraminyl hydrolase, EC 3.2.1.18) from the influenza virus A/Hong Kong/68 (H3N2) was purified after treatment of the purified virus with sarcosyl (sodium laurylsarcosinate) centrifugation at 110 000 × g, and chromatography on DEAE-Sephadex and Sephadex G-200. It migrated as a single component during electrophoresis on polyacrylamide gel, and its molecular weight was estimated about 270 000.The enzyme was thermolabile, the activity being reduced to 60% in 10 min at 50°C. The purified neuraminidase had an apparent Km value of 4.1 · 10−3 M for 5-N-acetyl-2-O-(3-methoxyphenyl)-α-d-neuraminic acid and was able to release sialic acid with linkages α2–3, α2–6 and α2–8 (with very different efficiency) from fetuin, gangliosides, colominic acid, and bovine and porcine submaxillary mucines.The enzymic activity was measured by several procedures: (A) spectrophotometric determination at 340 nm of the NADH produced in the reaction catalysed by β-galactose dehydrogenase on β-galactose + NAD+, this β-galactose was the product released from lactose by β-galactosidase and lactose was the product of the neuraminidase activity on N-acetylneuraminyl-lactose; (B) determination of the colored quinone yielded by the liberated methoxyphenol with 4-aminoantipyrine (Santer, U.V., Yee-Foon, J. and Glick, M.C. (1978) Biochim. Biophys. Acta 523, 435–442); (C) periodate-thiobarbiturate procedures (Warren, L. (1959) J. Biol. Chem. 234, 1971–1975 or Aminoff, D. (1961) Biochem. J. 81, 384–391). Some peculiarities of these methods are discussed.</div>
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Neuraminidase from influenza virus A (H3N2). Specificity towards several substrates and procedure of activity determination

Neuraminidase from influenza virus A (H3N2). Specificity towards several substrates and procedure of activity determination

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English descriptors

Abstract

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