A simple procedure for the analysis of the structural proteins of influenza and parainfluenza viruses involving adsorption to erythrocytes
Identifieur interne : 002534 ( Main/Exploration ); précédent : 002533; suivant : 002535A simple procedure for the analysis of the structural proteins of influenza and parainfluenza viruses involving adsorption to erythrocytes
Auteurs : J. A. Cowley [Australie] ; G. A. Tannock [Australie] ; Richard D. Barry [Australie]Source :
- Journal of Virological Methods [ 0166-0934 ] ; 1984.
English descriptors
- Teeft :
- Adsorption, Adsorption procedure, Cell aggregates, Choppin, Compans, Cowley, Culture medium, Erythrocyte, Erythrocyte adsorption, Erythrocyte suspensions, Influenza, Influenza virus strains, Marker proteins, Mdck, Mdck cells, Parainfluenza, Parainfluenza viruses, Polypeptide, Room temperature, Structural proteins, Sucrose, Sucrose gradient, Virology, Virus, Virus adsorption, Virus proteins, Wide range.
Abstract
Abstract: A simple procedure for the analysis of the structural proteins of influenza and parainfluenza viruses utilizing adsorption to erythrocytes is described. The method involves virus growth in the presence of [35S]methionine, adsorption of clarified culture medium with a 0.5% suspension of either guinea-pig or chicken erythrocytes and analysis of the virus-erythrocyte aggregates by sodium dodecyl sulphate-polya-crylamide gel electrophoresis (SDS-PAGE). All of the structural proteins can be detected using this procedure, and the protein profiles of virus-adsorbed erythrocyte complexes compare extremely well with those of sucrose density gradient purified virus preparations.
Url:
DOI: 10.1016/0166-0934(84)90036-3
Affiliations:
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A." last="Cowley">J. A. Cowley</name><affiliation wicri:level="1"><country xml:lang="fr">Australie</country><wicri:regionArea>Faculty of Medicine, The University of Newcastle, David Maddison Clinical Sciences Building, Royal Newcastle Hospital, Newcastle NSW 2300</wicri:regionArea><wicri:noRegion>Newcastle NSW 2300</wicri:noRegion></affiliation></author><author><name sortKey="Tannock, G A" sort="Tannock, G A" uniqKey="Tannock G" first="G. A." last="Tannock">G. A. Tannock</name><affiliation wicri:level="1"><country xml:lang="fr">Australie</country><wicri:regionArea>Faculty of Medicine, The University of Newcastle, David Maddison Clinical Sciences Building, Royal Newcastle Hospital, Newcastle NSW 2300</wicri:regionArea><wicri:noRegion>Newcastle NSW 2300</wicri:noRegion></affiliation></author><author><name sortKey="Barry, Richard D" sort="Barry, Richard D" uniqKey="Barry R" first="Richard D." last="Barry">Richard D. Barry</name><affiliation wicri:level="1"><country xml:lang="fr">Australie</country><wicri:regionArea>Faculty of Medicine, The University of Newcastle, David Maddison Clinical Sciences Building, Royal Newcastle Hospital, Newcastle NSW 2300</wicri:regionArea><wicri:noRegion>Newcastle NSW 2300</wicri:noRegion></affiliation></author></analytic><monogr></monogr><series><title level="j">Journal of Virological Methods</title><title level="j" type="abbrev">VIRMET</title><idno type="ISSN">0166-0934</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1984">1984</date><biblScope unit="volume">8</biblScope><biblScope unit="issue">1–2</biblScope><biblScope unit="page" from="9">9</biblScope><biblScope unit="page" to="18">18</biblScope></imprint><idno type="ISSN">0166-0934</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0166-0934</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Adsorption</term><term>Adsorption procedure</term><term>Cell aggregates</term><term>Choppin</term><term>Compans</term><term>Cowley</term><term>Culture medium</term><term>Erythrocyte</term><term>Erythrocyte adsorption</term><term>Erythrocyte suspensions</term><term>Influenza</term><term>Influenza virus strains</term><term>Marker proteins</term><term>Mdck</term><term>Mdck cells</term><term>Parainfluenza</term><term>Parainfluenza viruses</term><term>Polypeptide</term><term>Room temperature</term><term>Structural proteins</term><term>Sucrose</term><term>Sucrose gradient</term><term>Virology</term><term>Virus</term><term>Virus adsorption</term><term>Virus proteins</term><term>Wide range</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: A simple procedure for the analysis of the structural proteins of influenza and parainfluenza viruses utilizing adsorption to erythrocytes is described. The method involves virus growth in the presence of [35S]methionine, adsorption of clarified culture medium with a 0.5% suspension of either guinea-pig or chicken erythrocytes and analysis of the virus-erythrocyte aggregates by sodium dodecyl sulphate-polya-crylamide gel electrophoresis (SDS-PAGE). All of the structural proteins can be detected using this procedure, and the protein profiles of virus-adsorbed erythrocyte complexes compare extremely well with those of sucrose density gradient purified virus preparations.</div></front></TEI><affiliations><list><country><li>Australie</li></country></list><tree><country name="Australie"><noRegion><name sortKey="Cowley, J A" sort="Cowley, J A" uniqKey="Cowley J" first="J. A." last="Cowley">J. A. Cowley</name></noRegion><name sortKey="Barry, Richard D" sort="Barry, Richard D" uniqKey="Barry R" first="Richard D." last="Barry">Richard D. Barry</name><name sortKey="Tannock, G A" sort="Tannock, G A" uniqKey="Tannock G" first="G. A." last="Tannock">G. A. Tannock</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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