Purification of neuraminidase from Influenza virus subtype H5N1

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dc.creator Tarigan, Simson
dc.creator Indryani, Risa
dc.creator ., Darminto
dc.creator Ignjatovic, Jagoda
dc.date 2013-05-07
dc.date.accessioned 2018-06-04T06:46:53Z
dc.date.available 2018-06-04T06:46:53Z
dc.date.issued 2013-05-07
dc.identifier http://medpub.litbang.pertanian.go.id/index.php/jitv/article/view/366
dc.identifier 10.14334/jitv.v14i1.366
dc.identifier.uri http://repository.pertanian.go.id/handle/123456789/2656
dc.description Influenza-virus neuraminidase plays vital role in the survival of the organisms. Vaccination of animals with this glycoprotein confers immune responses so that enable it to protect the animals from incoming infection. Supplementation of conventional vaccines with this glycoprotein increases the protection and longevity of the vaccine. Purified neuraminidase can also be used to develop serological tests for differentiation of serologically positive animals due to infection or to vaccination. In this study purification of neuraminidase from influenza virus subtype H5N1 was described. Triton x-100 and Octyl β-D-glucopyranoside were used to extract and diluted the glycoprotein membrane. The enzymatic activity of the neuraminidase was assayed using a fluorochrome substrate, 4-methylumbelliferyl-a-D-N-acetyl neuraminic acid, which was found to be simple, sensitive and suitable for the purification purpose. The neuraminidase was absorbed selectively on an oxamic-acid agarose column. The purity of neuraminidase eluted from this affinity column was high. A higher purity of the neuraminidase was obtained by further separation with gel filtration on Superdex-200. The purified neuraminidase was enzymatically active and did not contain any detectable haemagglutinin, either by haemagglutination assay or by monospecific antibodies raised against H5N1 hemagglutinin.  The purified neuraminidase was recognized strongly by antibodies raised against an internal but only weakly by that against C-terminal regions of the neuraminidase protein of H5N1-influenza virus. The purified neuraminidase was in tetrameric forms but dissociated into monomeric form on reducing condition, or mostly dimeric form on non-reducing SDS-PAGE. Key Words: Neuraminidase, Influenza, H5N1, Methylumbelliferyl, Oxamic-acid en-US
dc.format application/pdf
dc.language eng
dc.publisher Indonesian Animal Sciences Society en-US
dc.relation http://medpub.litbang.pertanian.go.id/index.php/jitv/article/view/366/375
dc.rights Copyright (c) 1970 Indonesian Journal of Animal and Veterinary Sciences en-US
dc.rights http://creativecommons.org/licenses/by/4.0 en-US
dc.source 2252-696X
dc.source 0853-7380
dc.source Indonesian Journal of Animal and Veterinary Sciences; Vol 14, No 1 (2009): MARCH 2009; p.75-82 en-US
dc.title Purification of neuraminidase from Influenza virus subtype H5N1 en-US
dc.type info:eu-repo/semantics/article
dc.type info:eu-repo/semantics/publishedVersion
dc.type Peer-reviewed Article en-US

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