Mixed anionic detergent/aliphatic alcohol-polyacrylamide gel electrophoresis alters the separation of proteins relative to conventional sodium dodecyl sulfate-polyacrylamide gel electrophoresis
Identifieur interne : 000F56 ( Istex/Checkpoint ); précédent : 000F55; suivant : 000F57Mixed anionic detergent/aliphatic alcohol-polyacrylamide gel electrophoresis alters the separation of proteins relative to conventional sodium dodecyl sulfate-polyacrylamide gel electrophoresis
Auteurs : Earl G. Brown [Canada]Source :
- Analytical Biochemistry [ 0003-2697 ] ; 1988.
English descriptors
- KwdEn :
- Teeft :
- Aceto chemical company, Aliphatic, Aliphatic alcohols, Alkyl, Alkyl group, Cell proteins, Cleveland peptide mapping, Comigrating proteins, Conventional right, Conventional sdspage, Conventional yields, Corresponding aliphatic chain length, Detergent composition, Detergent conditions, Detergent phase, Different proteins, Disease control, Dodecyl, Dodecyl sulfate, Effective size, Electrophoresis, Electrophoresis system, Electrophoretic, Electrophoretic effect, Electrophoretic mobility, Electrophoretic mobility patterns, Electrophoretic separation, Electrophoretic species, Ferguson plots, First dimension, Hemagglutinin, Hemagglutinin proteins, Hexadecyl sulfate, Influenza, Influenza cells, Influenza proteins, Influenza virus, Laboratory centre, Madin darby, Mobility, Molecular weight, Nonstructural protein, Octadecyl sulfate, Peptide, Peptide mapping, Protein, Protein bands, Protein separation, Protein standards, Prototype strains, Relative mobility, Relative order, Relative positions, Sdspage, Second dimension, Services division, Sodium dodecyl, Sodium dodecyl sulfate, Sodium hexadecyl sulfate, Sodium octadecyl sulfate, Sodium tetradecyl sulfate, Strain characterization, Sulfate, Tetradecyl, Tetradecyl sulfate, Upper tank buffer, Vande woude.
Abstract
Abstract: The order and relative mobility of proteins on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) is affected by unknown components that are differentially present in SDS preparations obtained from different sources [J. B. Swaney, G. F. Vande Woude, and H. L. Bachrach (1974) Anal. Biochem.58, 337–346]. The modified separation capabilities of such SDS preparations are useful but the use of this phenomenon in a controlled manner requires that the components responsible for the altered separation be identified. Accordingly, this paper describes a polyacrylamide gel electrophoresis system [mixed alcohol/detergent-polyacrylamide gel electrophoresis (MAD-PAGE)] that employs a mixture of alcohol and detergent instead of SDS alone to modify and enhance protein separation relative to conventional SDS-PAGE. A defined mixture consisting of four sulfated aklyl detergents (dodecyl sulfate, tetradecyl sulfate, hexadecyl sulfate, octadecyl sulfate) as well as the four alcohols of corresponding aliphatic chain length was found to be effective at duplicating the electrophoretic effect of USP-grade SDS and thus changed the relative order and position of polypeptides on electrophoresis relative to conventional SDS-PAGE. This method serves as an adjunct to conventional SDS-PAGE by providing another means of resolving proteins that are not normally resolved by SDS-PAGE. Further, it was found that MAD-PAGE is capable of resolving the NS1 protein of influenza virus into three fractions, whereas conventional SDS-PAGE yields one electrophoretic species. Reelectrophoresis of these novel NS1 bands by conventional SDS-PAGE indicated that they were not modified during MAD-PAGE and probably represented distinct molecular forms present in infected cells. The electrophoretic mobility patterns of the NS1 bands of influenza H3N2 strains were polymorphic on MAD-PAGE and thus could be used as a means of strain characterization. MAD-PAGE was shown to be a useful means of protein separation and strain characterization for influenza viral proteins.
Url:
DOI: 10.1016/0003-2697(88)90555-6
Affiliations:
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<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">Mixed anionic detergent/aliphatic alcohol-polyacrylamide gel electrophoresis alters the separation of proteins relative to conventional sodium dodecyl sulfate-polyacrylamide gel electrophoresis</title><author><name sortKey="Brown, Earl G" sort="Brown, Earl G" uniqKey="Brown E" first="Earl G." last="Brown">Earl G. Brown</name></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:9978289126A1709888A1DA6DF42A1C8B0ED3F10F</idno><date when="1988" year="1988">1988</date><idno type="doi">10.1016/0003-2697(88)90555-6</idno><idno type="url">https://api.istex.fr/ark:/67375/6H6-3PDXJLFQ-3/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">000C03</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">000C03</idno><idno type="wicri:Area/Istex/Curation">000C03</idno><idno type="wicri:Area/Istex/Checkpoint">000F56</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Checkpoint">000F56</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">Mixed anionic detergent/aliphatic alcohol-polyacrylamide gel electrophoresis alters the separation of proteins relative to conventional sodium dodecyl sulfate-polyacrylamide gel electrophoresis</title><author><name sortKey="Brown, Earl G" sort="Brown, Earl G" uniqKey="Brown E" first="Earl G." last="Brown">Earl G. Brown</name><affiliation wicri:level="1"><country>Canada</country><wicri:regionArea>Influenza Section, Viral Diagnostic Services Division, Bureau of Microbiology, Laboratory Centre for Disease Control, Health and Welfare Canada, Ottawa, Ontario</wicri:regionArea><wicri:noRegion>Ontario</wicri:noRegion></affiliation></author></analytic><monogr></monogr><series><title level="j">Analytical Biochemistry</title><title level="j" type="abbrev">YABIO</title><idno type="ISSN">0003-2697</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1988">1988</date><biblScope unit="volume">174</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="337">337</biblScope><biblScope unit="page" to="348">348</biblScope></imprint><idno type="ISSN">0003-2697</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0003-2697</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>aliphatic alcohols</term><term>detergents</term><term>gel electrophoresis</term><term>influenza proteins</term></keywords><keywords scheme="Teeft" xml:lang="en"><term>Aceto chemical company</term><term>Aliphatic</term><term>Aliphatic alcohols</term><term>Alkyl</term><term>Alkyl group</term><term>Cell proteins</term><term>Cleveland peptide mapping</term><term>Comigrating proteins</term><term>Conventional right</term><term>Conventional sdspage</term><term>Conventional yields</term><term>Corresponding aliphatic chain length</term><term>Detergent composition</term><term>Detergent conditions</term><term>Detergent phase</term><term>Different proteins</term><term>Disease control</term><term>Dodecyl</term><term>Dodecyl sulfate</term><term>Effective size</term><term>Electrophoresis</term><term>Electrophoresis system</term><term>Electrophoretic</term><term>Electrophoretic effect</term><term>Electrophoretic mobility</term><term>Electrophoretic mobility patterns</term><term>Electrophoretic separation</term><term>Electrophoretic species</term><term>Ferguson plots</term><term>First dimension</term><term>Hemagglutinin</term><term>Hemagglutinin proteins</term><term>Hexadecyl sulfate</term><term>Influenza</term><term>Influenza cells</term><term>Influenza proteins</term><term>Influenza virus</term><term>Laboratory centre</term><term>Madin darby</term><term>Mobility</term><term>Molecular weight</term><term>Nonstructural protein</term><term>Octadecyl sulfate</term><term>Peptide</term><term>Peptide mapping</term><term>Protein</term><term>Protein bands</term><term>Protein separation</term><term>Protein standards</term><term>Prototype strains</term><term>Relative mobility</term><term>Relative order</term><term>Relative positions</term><term>Sdspage</term><term>Second dimension</term><term>Services division</term><term>Sodium dodecyl</term><term>Sodium dodecyl sulfate</term><term>Sodium hexadecyl sulfate</term><term>Sodium octadecyl sulfate</term><term>Sodium tetradecyl sulfate</term><term>Strain characterization</term><term>Sulfate</term><term>Tetradecyl</term><term>Tetradecyl sulfate</term><term>Upper tank buffer</term><term>Vande woude</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The order and relative mobility of proteins on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) is affected by unknown components that are differentially present in SDS preparations obtained from different sources [J. B. Swaney, G. F. Vande Woude, and H. L. Bachrach (1974) Anal. Biochem.58, 337–346]. The modified separation capabilities of such SDS preparations are useful but the use of this phenomenon in a controlled manner requires that the components responsible for the altered separation be identified. Accordingly, this paper describes a polyacrylamide gel electrophoresis system [mixed alcohol/detergent-polyacrylamide gel electrophoresis (MAD-PAGE)] that employs a mixture of alcohol and detergent instead of SDS alone to modify and enhance protein separation relative to conventional SDS-PAGE. A defined mixture consisting of four sulfated aklyl detergents (dodecyl sulfate, tetradecyl sulfate, hexadecyl sulfate, octadecyl sulfate) as well as the four alcohols of corresponding aliphatic chain length was found to be effective at duplicating the electrophoretic effect of USP-grade SDS and thus changed the relative order and position of polypeptides on electrophoresis relative to conventional SDS-PAGE. This method serves as an adjunct to conventional SDS-PAGE by providing another means of resolving proteins that are not normally resolved by SDS-PAGE. Further, it was found that MAD-PAGE is capable of resolving the NS1 protein of influenza virus into three fractions, whereas conventional SDS-PAGE yields one electrophoretic species. Reelectrophoresis of these novel NS1 bands by conventional SDS-PAGE indicated that they were not modified during MAD-PAGE and probably represented distinct molecular forms present in infected cells. The electrophoretic mobility patterns of the NS1 bands of influenza H3N2 strains were polymorphic on MAD-PAGE and thus could be used as a means of strain characterization. MAD-PAGE was shown to be a useful means of protein separation and strain characterization for influenza viral proteins.</div></front></TEI><affiliations><list><country><li>Canada</li></country></list><tree><country name="Canada"><noRegion><name sortKey="Brown, Earl G" sort="Brown, Earl G" uniqKey="Brown E" first="Earl G." last="Brown">Earl G. Brown</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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