Purification strategies for sendai virus membrane proteins
Identifieur interne : 001D09 ( Main/Exploration ); précédent : 001D08; suivant : 001D10Purification strategies for sendai virus membrane proteins
Auteurs : Gjalt W. Welling [Pays-Bas] ; Kunja Slopsema [Pays-Bas] ; Sytske Welling-Wester [Pays-Bas]Source :
- Journal of Chromatography A [ 0021-9673 ] ; 1987.
English descriptors
- Teeft :
- Amino acids, Ammonium chloride, Average membrane protein, Average protein, Broad peaks, Chelate, Column matrix, Different gradient programs, Dimer, Disulfide bridge, Elution buffer, Elution pattern, First program, Fusion protein, Hplc, Hydrophobic membrane proteins, Integral membrane proteins, Kilodaltons, Liquid chromatography, Membrane proteins, Metal chelate affinity hplc, Molecular weight, Molecular weights, Phenyl column, Present study, Protein, Reference proteins, Same elution conditions, Second program, Sendai, Sendai virions, Sendai virus, Sendai virus membrane, Sendai virus membrane proteins, Sendai virus proteins, Slopsema, Sodium acetate, Sodium chloride, Sodium dodecyl sulphate, Sodium phosphate, Tetramer, Toyo soda, Triton, Zinc chloride.
Abstract
Abstract: Viral membrane proteins extracted from Sendai virions with the non-ionic detergents decylpolyethyleneglycol-300 and Triton X-100 were used as a model mixture of hydrophobic membrane proteins. The detergent extract contained the fusion protein (F) and the tetrameric and dimeric forms of the hemagglutinin-neuraminidase protein (HN). These proteins were purified by size-exclusion high-performance liquid chromatography (HPLC) in the presence of 0.1% sodium dodecyl sulphate, by ion-exchange and metal chelate affinity HPLC in the presence of 0.1% decylpolyethyleneglycol, and by reversed-phase HPLC without prior removal of the detergent. The tetramer of HN and F could be purified by size-exclusion HPLC after dissociation of a micellar aggregate containing tetrameric HN and multimeric F. The F and HN proteins could be purified by ion-exchange HPLC. Pure F protein could be obtained after metal chelate affinity HPLC. The F protein and the dimer and tetramer of HN could be eluted from a large-pore (100 nm) reversed-phase column, but they were eluted as broad, overlapping peaks. Only after reduction of the virion extract, the relatively small (13–15 kilodaltons) F2 protein could be obtained in pure form.
Url:
DOI: 10.1016/S0021-9673(01)84999-2
Affiliations:
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Welling</name></author><author><name sortKey="Slopsema, Kunja" sort="Slopsema, Kunja" uniqKey="Slopsema K" first="Kunja" last="Slopsema">Kunja Slopsema</name></author><author><name sortKey="Welling Wester, Sytske" sort="Welling Wester, Sytske" uniqKey="Welling Wester S" first="Sytske" last="Welling-Wester">Sytske Welling-Wester</name></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:B644B98362610955154225D9FD328982B434A060</idno><date when="1987" year="1987">1987</date><idno type="doi">10.1016/S0021-9673(01)84999-2</idno><idno type="url">https://api.istex.fr/ark:/67375/6H6-79R5ND4X-R/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">000540</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">000540</idno><idno type="wicri:Area/Istex/Curation">000507</idno><idno type="wicri:Area/Istex/Checkpoint">000680</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Checkpoint">000680</idno><idno type="wicri:doubleKey">0021-9673:1987:Welling G:purification:strategies:for</idno><idno type="wicri:Area/Main/Merge">001D31</idno><idno type="wicri:Area/Main/Curation">001D09</idno><idno type="wicri:Area/Main/Exploration">001D09</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a">Purification strategies for sendai virus membrane proteins</title><author><name sortKey="Welling, Gjalt W" sort="Welling, Gjalt W" uniqKey="Welling G" first="Gjalt W." last="Welling">Gjalt W. Welling</name><affiliation wicri:level="4"><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>Laboratorium voor Medische Microbiologie, Rijksuniversiteit Groningen, Oostersingel 59</wicri:regionArea><orgName type="university">Université de Groningue</orgName><placeName><settlement type="city">Groningue (ville)</settlement><region>Groningue (province)</region></placeName></affiliation></author><author><name sortKey="Slopsema, Kunja" sort="Slopsema, Kunja" uniqKey="Slopsema K" first="Kunja" last="Slopsema">Kunja Slopsema</name><affiliation wicri:level="4"><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>Laboratorium voor Medische Microbiologie, Rijksuniversiteit Groningen, Oostersingel 59</wicri:regionArea><orgName type="university">Université de Groningue</orgName><placeName><settlement type="city">Groningue (ville)</settlement><region>Groningue (province)</region></placeName></affiliation></author><author><name sortKey="Welling Wester, Sytske" sort="Welling Wester, Sytske" uniqKey="Welling Wester S" first="Sytske" last="Welling-Wester">Sytske Welling-Wester</name><affiliation wicri:level="4"><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>Laboratorium voor Medische Microbiologie, Rijksuniversiteit Groningen, Oostersingel 59</wicri:regionArea><orgName type="university">Université de Groningue</orgName><placeName><settlement type="city">Groningue (ville)</settlement><region>Groningue (province)</region></placeName></affiliation></author></analytic><monogr></monogr><series><title level="j">Journal of Chromatography A</title><title level="j" type="abbrev">CHROMA</title><idno type="ISSN">0021-9673</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1987">1987</date><biblScope unit="volume">397</biblScope><biblScope unit="supplement">C</biblScope><biblScope unit="page" from="165">165</biblScope><biblScope unit="page" to="174">174</biblScope></imprint><idno type="ISSN">0021-9673</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0021-9673</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Amino acids</term><term>Ammonium chloride</term><term>Average membrane protein</term><term>Average protein</term><term>Broad peaks</term><term>Chelate</term><term>Column matrix</term><term>Different gradient programs</term><term>Dimer</term><term>Disulfide bridge</term><term>Elution buffer</term><term>Elution pattern</term><term>First program</term><term>Fusion protein</term><term>Hplc</term><term>Hydrophobic membrane proteins</term><term>Integral membrane proteins</term><term>Kilodaltons</term><term>Liquid chromatography</term><term>Membrane proteins</term><term>Metal chelate affinity hplc</term><term>Molecular weight</term><term>Molecular weights</term><term>Phenyl column</term><term>Present study</term><term>Protein</term><term>Reference proteins</term><term>Same elution conditions</term><term>Second program</term><term>Sendai</term><term>Sendai virions</term><term>Sendai virus</term><term>Sendai virus membrane</term><term>Sendai virus membrane proteins</term><term>Sendai virus proteins</term><term>Slopsema</term><term>Sodium acetate</term><term>Sodium chloride</term><term>Sodium dodecyl sulphate</term><term>Sodium phosphate</term><term>Tetramer</term><term>Toyo soda</term><term>Triton</term><term>Zinc chloride</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Viral membrane proteins extracted from Sendai virions with the non-ionic detergents decylpolyethyleneglycol-300 and Triton X-100 were used as a model mixture of hydrophobic membrane proteins. The detergent extract contained the fusion protein (F) and the tetrameric and dimeric forms of the hemagglutinin-neuraminidase protein (HN). These proteins were purified by size-exclusion high-performance liquid chromatography (HPLC) in the presence of 0.1% sodium dodecyl sulphate, by ion-exchange and metal chelate affinity HPLC in the presence of 0.1% decylpolyethyleneglycol, and by reversed-phase HPLC without prior removal of the detergent. The tetramer of HN and F could be purified by size-exclusion HPLC after dissociation of a micellar aggregate containing tetrameric HN and multimeric F. The F and HN proteins could be purified by ion-exchange HPLC. Pure F protein could be obtained after metal chelate affinity HPLC. The F protein and the dimer and tetramer of HN could be eluted from a large-pore (100 nm) reversed-phase column, but they were eluted as broad, overlapping peaks. Only after reduction of the virion extract, the relatively small (13–15 kilodaltons) F2 protein could be obtained in pure form.</div></front></TEI><affiliations><list><country><li>Pays-Bas</li></country><region><li>Groningue (province)</li></region><settlement><li>Groningue (ville)</li></settlement><orgName><li>Université de Groningue</li></orgName></list><tree><country name="Pays-Bas"><region name="Groningue (province)"><name sortKey="Welling, Gjalt W" sort="Welling, Gjalt W" uniqKey="Welling G" first="Gjalt W." last="Welling">Gjalt W. Welling</name></region><name sortKey="Slopsema, Kunja" sort="Slopsema, Kunja" uniqKey="Slopsema K" first="Kunja" last="Slopsema">Kunja Slopsema</name><name sortKey="Welling Wester, Sytske" sort="Welling Wester, Sytske" uniqKey="Welling Wester S" first="Sytske" last="Welling-Wester">Sytske Welling-Wester</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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