Further evidence for multiple proteins in the foot-and-mouth disease virus particle
Animal Virus Research Institute, Pirbright, Surrey Further evidence has been obtained which confirms that foot-and-mouth disease virus contains several structural proteins. By electrophoresis in urea-polyacrylamide gels, virus of type O gave six distinct bands. In sodium dodecyl sulphate-polyacrylam...
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| Veröffentlicht in: | Journal of general virology 1971-10, Vol.13 (1), p.73-84 |
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| container_title | Journal of general virology |
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| creator | Burroughs, J.N Rowlands, D.J Sangar, D.V Talbot, P Brown, F |
| description | Animal Virus Research Institute, Pirbright, Surrey
Further evidence has been obtained which confirms that foot-and-mouth disease virus contains several structural proteins. By electrophoresis in urea-polyacrylamide gels, virus of type O gave six distinct bands. In sodium dodecyl sulphate-polyacrylamide gels four proteins with molecular weights of 34, 30, 26 and 13.5 x 10 3 were clearly demonstrated. When virus preparations were labelled with a single amino acid, in both sodium dodecyl sulphate-polyacrylamide and urea-polyacrylamide gel electrophoresis, the fastest migrating protein contained no arginine and only traces of cysteine. This protein also stained differently from the other bands with Coomassie Blue and was absent from the 12s protein subunit prepared by mild acid (pH 6.5) disruption of the virus. This protein was separated from the 12s subunit by sucrose gradient centrifugation and by ion exchange chromatography on Amberlite IRC-50.
Received 8 March 1971;
accepted 1 June 1971. |
| doi_str_mv | 10.1099/0022-1317-13-1-73 |
| format | Article |
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Further evidence has been obtained which confirms that foot-and-mouth disease virus contains several structural proteins. By electrophoresis in urea-polyacrylamide gels, virus of type O gave six distinct bands. In sodium dodecyl sulphate-polyacrylamide gels four proteins with molecular weights of 34, 30, 26 and 13.5 x 10 3 were clearly demonstrated. When virus preparations were labelled with a single amino acid, in both sodium dodecyl sulphate-polyacrylamide and urea-polyacrylamide gel electrophoresis, the fastest migrating protein contained no arginine and only traces of cysteine. This protein also stained differently from the other bands with Coomassie Blue and was absent from the 12s protein subunit prepared by mild acid (pH 6.5) disruption of the virus. This protein was separated from the 12s subunit by sucrose gradient centrifugation and by ion exchange chromatography on Amberlite IRC-50.
Received 8 March 1971;
accepted 1 June 1971.</description><identifier>ISSN: 0022-1317</identifier><identifier>EISSN: 1465-2099</identifier><identifier>DOI: 10.1099/0022-1317-13-1-73</identifier><identifier>PMID: 4108674</identifier><language>eng</language><publisher>England: Soc General Microbiol</publisher><subject>Amino Acids - analysis ; animal diseases ; animal health ; Animals ; Aphthovirus - analysis ; Aphthovirus - growth & development ; Azo Compounds ; Carbon Isotopes ; Cattle ; Cell Line ; Centrifugation, Density Gradient ; Chromatography, Ion Exchange ; Cricetinae ; Culture Techniques ; Electrophoresis, Disc ; Hydrogen-Ion Concentration ; Isoelectric Focusing ; Kidney ; Molecular Weight ; Peptides - analysis ; Sodium ; Staining and Labeling ; Sucrose ; Sulfates ; Tritium ; Trypsin ; Urea ; Uridine ; Viral Proteins - analysis ; Viral Proteins - isolation & purification</subject><ispartof>Journal of general virology, 1971-10, Vol.13 (1), p.73-84</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c394t-6e681bfe19ae69b4e630c377134d69a7398112054bb9929236f9b7ee8f277d653</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,3746,3747,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/4108674$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Burroughs, J.N</creatorcontrib><creatorcontrib>Rowlands, D.J</creatorcontrib><creatorcontrib>Sangar, D.V</creatorcontrib><creatorcontrib>Talbot, P</creatorcontrib><creatorcontrib>Brown, F</creatorcontrib><title>Further evidence for multiple proteins in the foot-and-mouth disease virus particle</title><title>Journal of general virology</title><addtitle>J Gen Virol</addtitle><description>Animal Virus Research Institute, Pirbright, Surrey
Further evidence has been obtained which confirms that foot-and-mouth disease virus contains several structural proteins. By electrophoresis in urea-polyacrylamide gels, virus of type O gave six distinct bands. In sodium dodecyl sulphate-polyacrylamide gels four proteins with molecular weights of 34, 30, 26 and 13.5 x 10 3 were clearly demonstrated. When virus preparations were labelled with a single amino acid, in both sodium dodecyl sulphate-polyacrylamide and urea-polyacrylamide gel electrophoresis, the fastest migrating protein contained no arginine and only traces of cysteine. This protein also stained differently from the other bands with Coomassie Blue and was absent from the 12s protein subunit prepared by mild acid (pH 6.5) disruption of the virus. This protein was separated from the 12s subunit by sucrose gradient centrifugation and by ion exchange chromatography on Amberlite IRC-50.
Received 8 March 1971;
accepted 1 June 1971.</description><subject>Amino Acids - analysis</subject><subject>animal diseases</subject><subject>animal health</subject><subject>Animals</subject><subject>Aphthovirus - analysis</subject><subject>Aphthovirus - growth & development</subject><subject>Azo Compounds</subject><subject>Carbon Isotopes</subject><subject>Cattle</subject><subject>Cell Line</subject><subject>Centrifugation, Density Gradient</subject><subject>Chromatography, Ion Exchange</subject><subject>Cricetinae</subject><subject>Culture Techniques</subject><subject>Electrophoresis, Disc</subject><subject>Hydrogen-Ion Concentration</subject><subject>Isoelectric Focusing</subject><subject>Kidney</subject><subject>Molecular Weight</subject><subject>Peptides - analysis</subject><subject>Sodium</subject><subject>Staining and Labeling</subject><subject>Sucrose</subject><subject>Sulfates</subject><subject>Tritium</subject><subject>Trypsin</subject><subject>Urea</subject><subject>Uridine</subject><subject>Viral Proteins - analysis</subject><subject>Viral Proteins - isolation & purification</subject><issn>0022-1317</issn><issn>1465-2099</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1971</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkDtPAzEQhC0EgvD4ARQIV3QGr-3Y5xIhXhISBVBbvru9xOgewb4D8e9xlCg0u8XMzo4-Qs6BXwO39oZzIRhIMHkwYEbukRkoPWciq_tkttOPyHFKn5yDUnNzSA4V8EIbNSNvD1Mclxgpfoca-wppM0TaTe0YVi3SVRxGDH2ioafZlsVhZL6vWTdM45LWIaFPSL9DnBJd-TiGqsVTctD4NuHZdp-Qj4f797sn9vL6-Hx3-8IqadXINOoCygbBetS2VKglr6QxIFWtrTfSFgCCz1VZWiuskLqxpUEsGmFMrefyhFxtcnPLrwnT6LqQKmxb3-MwJVeAENIom42wMVZxSCli41YxdD7-OuBuDdKtQbk1qDwcOCPzzcU2fCo7rHcXW3L_z5dhsfwJEd0C-y7kD2UYXAbyH3S5MTZ-cH4RQ3Ifb4KD5AAy1-PyD11shGg</recordid><startdate>197110</startdate><enddate>197110</enddate><creator>Burroughs, J.N</creator><creator>Rowlands, D.J</creator><creator>Sangar, D.V</creator><creator>Talbot, P</creator><creator>Brown, F</creator><general>Soc General Microbiol</general><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>197110</creationdate><title>Further evidence for multiple proteins in the foot-and-mouth disease virus particle</title><author>Burroughs, J.N ; Rowlands, D.J ; Sangar, D.V ; Talbot, P ; Brown, F</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c394t-6e681bfe19ae69b4e630c377134d69a7398112054bb9929236f9b7ee8f277d653</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1971</creationdate><topic>Amino Acids - analysis</topic><topic>animal diseases</topic><topic>animal health</topic><topic>Animals</topic><topic>Aphthovirus - analysis</topic><topic>Aphthovirus - growth & development</topic><topic>Azo Compounds</topic><topic>Carbon Isotopes</topic><topic>Cattle</topic><topic>Cell Line</topic><topic>Centrifugation, Density Gradient</topic><topic>Chromatography, Ion Exchange</topic><topic>Cricetinae</topic><topic>Culture Techniques</topic><topic>Electrophoresis, Disc</topic><topic>Hydrogen-Ion Concentration</topic><topic>Isoelectric Focusing</topic><topic>Kidney</topic><topic>Molecular Weight</topic><topic>Peptides - analysis</topic><topic>Sodium</topic><topic>Staining and Labeling</topic><topic>Sucrose</topic><topic>Sulfates</topic><topic>Tritium</topic><topic>Trypsin</topic><topic>Urea</topic><topic>Uridine</topic><topic>Viral Proteins - analysis</topic><topic>Viral Proteins - isolation & purification</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Burroughs, J.N</creatorcontrib><creatorcontrib>Rowlands, D.J</creatorcontrib><creatorcontrib>Sangar, D.V</creatorcontrib><creatorcontrib>Talbot, P</creatorcontrib><creatorcontrib>Brown, F</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of general virology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Burroughs, J.N</au><au>Rowlands, D.J</au><au>Sangar, D.V</au><au>Talbot, P</au><au>Brown, F</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Further evidence for multiple proteins in the foot-and-mouth disease virus particle</atitle><jtitle>Journal of general virology</jtitle><addtitle>J Gen Virol</addtitle><date>1971-10</date><risdate>1971</risdate><volume>13</volume><issue>1</issue><spage>73</spage><epage>84</epage><pages>73-84</pages><issn>0022-1317</issn><eissn>1465-2099</eissn><abstract>Animal Virus Research Institute, Pirbright, Surrey
Further evidence has been obtained which confirms that foot-and-mouth disease virus contains several structural proteins. By electrophoresis in urea-polyacrylamide gels, virus of type O gave six distinct bands. In sodium dodecyl sulphate-polyacrylamide gels four proteins with molecular weights of 34, 30, 26 and 13.5 x 10 3 were clearly demonstrated. When virus preparations were labelled with a single amino acid, in both sodium dodecyl sulphate-polyacrylamide and urea-polyacrylamide gel electrophoresis, the fastest migrating protein contained no arginine and only traces of cysteine. This protein also stained differently from the other bands with Coomassie Blue and was absent from the 12s protein subunit prepared by mild acid (pH 6.5) disruption of the virus. This protein was separated from the 12s subunit by sucrose gradient centrifugation and by ion exchange chromatography on Amberlite IRC-50.
Received 8 March 1971;
accepted 1 June 1971.</abstract><cop>England</cop><pub>Soc General Microbiol</pub><pmid>4108674</pmid><doi>10.1099/0022-1317-13-1-73</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Journal of general virology, 1971-10, Vol.13 (1), p.73-84 |
| issn | 0022-1317 1465-2099 |
| language | eng |
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| source | MEDLINE; Microbiology Society; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Amino Acids - analysis animal diseases animal health Animals Aphthovirus - analysis Aphthovirus - growth & development Azo Compounds Carbon Isotopes Cattle Cell Line Centrifugation, Density Gradient Chromatography, Ion Exchange Cricetinae Culture Techniques Electrophoresis, Disc Hydrogen-Ion Concentration Isoelectric Focusing Kidney Molecular Weight Peptides - analysis Sodium Staining and Labeling Sucrose Sulfates Tritium Trypsin Urea Uridine Viral Proteins - analysis Viral Proteins - isolation & purification |
| title | Further evidence for multiple proteins in the foot-and-mouth disease virus particle |
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