Electrophoretic separation and characterization of subunits released from influenza virus by detergents.
Identifieur interne : 000642 ( PubMed/Corpus ); précédent : 000641; suivant : 000643Electrophoretic separation and characterization of subunits released from influenza virus by detergents.
Auteurs : G. Russ ; G. Ruttkay-Nedecky ; V. MuchaSource :
- Acta virologica [ 0001-723X ] ; 1976.
English descriptors
- KwdEn :
- Electrophoresis, Polyacrylamide Gel, Ethyl Ethers (pharmacology), Hemagglutinins, Viral (analysis), Neuraminidase (analysis), Orthomyxoviridae (analysis), Orthomyxoviridae (drug effects), Polyethylene Glycols (pharmacology), RNA, Viral (analysis), Sodium Dodecyl Sulfate (pharmacology), Viral Proteins (analysis).
- MESH :
- chemical , analysis : Hemagglutinins, Viral, Neuraminidase, RNA, Viral, Viral Proteins.
- chemical , pharmacology : Ethyl Ethers, Polyethylene Glycols, Sodium Dodecyl Sulfate.
- analysis : Orthomyxoviridae.
- drug effects : Orthomyxoviridae.
- Electrophoresis, Polyacrylamide Gel.
Abstract
Subunits released from influenza A/Singapore/1/57 (H2N2) virus by either Triton-X-100 (T-X-100); or sodium lauryl sarcosinate (SLS) or ether were separated by electrophoresis in agarose suspension into a rapidly migrating fraction (I) and a slowly migrating fraction (II). Fraction I obtained after T-X-100 treatment contained the viral ribonucleoprotein (RNP) in a form indistinguishable from the obtained after ether treatment. SLS treatment of the virus resulted in a rapidly migrating fraction containing only the protein part of the viral RNP. Fraction II obtained after T-X-100 or SLS treatment contained both haemagglutinin (HA) and neuraminidase (NA), mostly dissociated from each other, in contrast to fraction II obtained after ether treatment which contained mixed aggregates of HA and NA. The yields of electrophoretically isolated RNP and HA-NA were essentially the same irrespective of whether T-X-100 or ether was used for virus disruption. Treatment of virus by T-X-100 and subsequent removal of the latter resulted in a 10-20-fold increase of the HA activity. After sodium dodecyl sulphate (SDS) treatment of the virus, the NA activity was found in a heterogeneous fraction with surprisingly high migration rate towards the anode, indicating that NA remained active despite its extensive SDS binding.
PubMed: 7935
Links to Exploration step
pubmed:7935Le document en format XML
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Mucha</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1976">1976</date><idno type="RBID">pubmed:7935</idno><idno type="pmid">7935</idno><idno type="wicri:Area/PubMed/Corpus">000642</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000642</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Electrophoretic separation and characterization of subunits released from influenza virus by detergents.</title><author><name sortKey="Russ, G" sort="Russ, G" uniqKey="Russ G" first="G" last="Russ">G. Russ</name></author><author><name sortKey="Ruttkay Nedecky, G" sort="Ruttkay Nedecky, G" uniqKey="Ruttkay Nedecky G" first="G" last="Ruttkay-Nedecky">G. Ruttkay-Nedecky</name></author><author><name sortKey="Mucha, V" sort="Mucha, V" uniqKey="Mucha V" first="V" last="Mucha">V. Mucha</name></author></analytic><series><title level="j">Acta virologica</title><idno type="ISSN">0001-723X</idno><imprint><date when="1976" type="published">1976</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Electrophoresis, Polyacrylamide Gel</term><term>Ethyl Ethers (pharmacology)</term><term>Hemagglutinins, Viral (analysis)</term><term>Neuraminidase (analysis)</term><term>Orthomyxoviridae (analysis)</term><term>Orthomyxoviridae (drug effects)</term><term>Polyethylene Glycols (pharmacology)</term><term>RNA, Viral (analysis)</term><term>Sodium Dodecyl Sulfate (pharmacology)</term><term>Viral Proteins (analysis)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Hemagglutinins, Viral</term><term>Neuraminidase</term><term>RNA, Viral</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Ethyl Ethers</term><term>Polyethylene Glycols</term><term>Sodium Dodecyl Sulfate</term></keywords><keywords scheme="MESH" qualifier="analysis" xml:lang="en"><term>Orthomyxoviridae</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Orthomyxoviridae</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Electrophoresis, Polyacrylamide Gel</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Subunits released from influenza A/Singapore/1/57 (H2N2) virus by either Triton-X-100 (T-X-100); or sodium lauryl sarcosinate (SLS) or ether were separated by electrophoresis in agarose suspension into a rapidly migrating fraction (I) and a slowly migrating fraction (II). Fraction I obtained after T-X-100 treatment contained the viral ribonucleoprotein (RNP) in a form indistinguishable from the obtained after ether treatment. SLS treatment of the virus resulted in a rapidly migrating fraction containing only the protein part of the viral RNP. Fraction II obtained after T-X-100 or SLS treatment contained both haemagglutinin (HA) and neuraminidase (NA), mostly dissociated from each other, in contrast to fraction II obtained after ether treatment which contained mixed aggregates of HA and NA. The yields of electrophoretically isolated RNP and HA-NA were essentially the same irrespective of whether T-X-100 or ether was used for virus disruption. Treatment of virus by T-X-100 and subsequent removal of the latter resulted in a 10-20-fold increase of the HA activity. After sodium dodecyl sulphate (SDS) treatment of the virus, the NA activity was found in a heterogeneous fraction with surprisingly high migration rate towards the anode, indicating that NA remained active despite its extensive SDS binding.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">7935</PMID><DateCompleted><Year>1976</Year><Month>10</Month><Day>02</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>30</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0001-723X</ISSN><JournalIssue CitedMedium="Print"><Volume>20</Volume><Issue>1</Issue><PubDate><Year>1976</Year><Month>Feb</Month></PubDate></JournalIssue><Title>Acta virologica</Title><ISOAbbreviation>Acta Virol.</ISOAbbreviation></Journal><ArticleTitle>Electrophoretic separation and characterization of subunits released from influenza virus by detergents.</ArticleTitle><Pagination><MedlinePgn>1-8</MedlinePgn></Pagination><Abstract><AbstractText>Subunits released from influenza A/Singapore/1/57 (H2N2) virus by either Triton-X-100 (T-X-100); or sodium lauryl sarcosinate (SLS) or ether were separated by electrophoresis in agarose suspension into a rapidly migrating fraction (I) and a slowly migrating fraction (II). Fraction I obtained after T-X-100 treatment contained the viral ribonucleoprotein (RNP) in a form indistinguishable from the obtained after ether treatment. SLS treatment of the virus resulted in a rapidly migrating fraction containing only the protein part of the viral RNP. Fraction II obtained after T-X-100 or SLS treatment contained both haemagglutinin (HA) and neuraminidase (NA), mostly dissociated from each other, in contrast to fraction II obtained after ether treatment which contained mixed aggregates of HA and NA. The yields of electrophoretically isolated RNP and HA-NA were essentially the same irrespective of whether T-X-100 or ether was used for virus disruption. Treatment of virus by T-X-100 and subsequent removal of the latter resulted in a 10-20-fold increase of the HA activity. After sodium dodecyl sulphate (SDS) treatment of the virus, the NA activity was found in a heterogeneous fraction with surprisingly high migration rate towards the anode, indicating that NA remained active despite its extensive SDS binding.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Russ</LastName><ForeName>G</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Ruttkay-Nedecky</LastName><ForeName>G</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Mucha</LastName><ForeName>V</ForeName><Initials>V</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Slovakia</Country><MedlineTA>Acta Virol</MedlineTA><NlmUniqueID>0370401</NlmUniqueID><ISSNLinking>0001-723X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005019">Ethyl Ethers</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D006389">Hemagglutinins, Viral</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012367">RNA, Viral</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014764">Viral Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>368GB5141J</RegistryNumber><NameOfSubstance UI="D012967">Sodium Dodecyl Sulfate</NameOfSubstance></Chemical><Chemical><RegistryNumber>3WJQ0SDW1A</RegistryNumber><NameOfSubstance UI="D011092">Polyethylene Glycols</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.18</RegistryNumber><NameOfSubstance UI="D009439">Neuraminidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D004591" MajorTopicYN="N">Electrophoresis, Polyacrylamide Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005019" MajorTopicYN="N">Ethyl Ethers</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006389" MajorTopicYN="N">Hemagglutinins, Viral</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009439" MajorTopicYN="N">Neuraminidase</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009975" MajorTopicYN="N">Orthomyxoviridae</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="Y">analysis</QualifierName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011092" MajorTopicYN="N">Polyethylene Glycols</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012367" MajorTopicYN="N">RNA, Viral</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="Y">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012967" MajorTopicYN="N">Sodium Dodecyl Sulfate</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014764" MajorTopicYN="N">Viral Proteins</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="Y">analysis</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1976</Year><Month>2</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1976</Year><Month>2</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1976</Year><Month>2</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">7935</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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