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https://repositorio.ufba.br/handle/ri/20341Registro completo de metadados
| Campo DC | Valor | Idioma |
|---|---|---|
| dc.contributor.author | Couto, Alessanda Abdo do | - |
| dc.contributor.author | Barros, José Júnior França de | - |
| dc.contributor.author | Couceiro, José Nelson dos Santos Silva | - |
| dc.creator | Couto, Alessanda Abdo do | - |
| dc.creator | Barros, José Júnior França de | - |
| dc.creator | Couceiro, José Nelson dos Santos Silva | - |
| dc.date.accessioned | 2016-09-13T15:08:36Z | - |
| dc.date.available | 2016-09-13T15:08:36Z | - |
| dc.date.issued | 2004 | - |
| dc.identifier.citation | COUTO, A. A. do. Receptor-binding variants of H3N2 influenza A viruses: characterization of their sialidase activity towards different substrates. R. Ci. méd. biol., Salvador, v. 3, n. 1, p. 13-19, jan./jun. 2004. | pt_BR |
| dc.identifier.issn | 2236-5222 | - |
| dc.identifier.uri | http://repositorio.ufba.br/ri/handle/ri/20341 | - |
| dc.description | Artigo original (p.13-19) | pt_BR |
| dc.description.abstract | Influenza virus sialidase develops an essential activity on cellular glycoproteins, then permitting the dissemination of the virus infections by preventing virus-virus self aggregation and virus-cell rebinding. Two purified variant samples of influenza A/Memphis/102/72 (H3N2) viruses, which are recognized for their receptor-binding activity to a-2,6 or a- 2,3-sialyllactose structures, were analysed for their sialidase activity on different natural and artificial substrates. The M1/ 5 sample exhibited higher sialidase activity on fetuin (O.D.=0.226), MPN (O.D.=0.110) and human erythrocytes (10,240 HAU/ml), while the activity of the M1/5HS8 sample on these substrates was expressed by O.D.=0.129, O.D.=0.065 and 2,560 HAU/ml when using fetuin, MPN and human erythrocytes as substrates, respectively. However, the M1/5HS8 sample showed more significative sialidase activity on mucin when compared to the M1/5 sample: the enzyme activity of first sample was responsible for liberation of 3.5 nmol of free sialic acids while the last one produced 16.5 nmol of free sialic acids | pt_BR |
| dc.language.iso | pt_BR | pt_BR |
| dc.publisher | Instituto de Ciências da Saúde/ Universidade Federal da Bahia | pt_BR |
| dc.rights | Acesso Aberto | pt_BR |
| dc.source | http://www.portalseer.ufba.br/index.php/cmbio/issue/view/498/showToc | pt_BR |
| dc.subject | Influenza virus. | pt_BR |
| dc.subject | Receptor-binding variants. | pt_BR |
| dc.subject | Neuraminidase (NA). | pt_BR |
| dc.subject | Natural and artificial substrates. | pt_BR |
| dc.title | Receptor-binding variants of H3N2 influenza A viruses: characterization of their sialidase activity towards different substrates | pt_BR |
| dc.title.alternative | Revista de Ciências Médicas e Biológicas | pt_BR |
| dc.type | Artigo de Periódico | pt_BR |
| dc.description.localpub | Salvador | pt_BR |
| dc.identifier.number | v.3, n.1 | pt_BR |
| Aparece nas coleções: | Artigo Publicado em Periódico (PPGPIOS) | |
Arquivos associados a este item:
| Arquivo | Descrição | Tamanho | Formato | |
|---|---|---|---|---|
| R. Ci. méd. biol., v.3, n. 1-2004.pdf_0 | 66,88 kB | Adobe PDF | Visualizar/Abrir |
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