Column liquid chromatography of integral membrane proteins
Identifieur interne : 001D23 ( Main/Exploration ); précédent : 001D22; suivant : 001D24Column liquid chromatography of integral membrane proteins
Auteurs : Gjalt W. Welling [Pays-Bas] ; Ruurd Van Der Zee [Pays-Bas] ; Sytske Welling-Wester [Pays-Bas]Source :
- Journal of Chromatography B: Biomedical Sciences and Applications [ 0378-4347 ] ; 1987.
English descriptors
- Teeft :
- Amino, Amino acids, Ammonium, Ammonium sulphate, Ammonium thiocyanate, Anal, Anal biochem, Aqueous phase, Average protein, Bilayer, Bile salts, Bioaffinity, Bioaffinity chromatography, Biochem, Biol, Biol chem, Biological activity, Biological applications, Biological processes, Buffer systems, Cell biol, Chem, Chromatogr, Chromatographic methodology, Chromatography, Coli, Coli contaminants, Column length, Column ligands, Corona virus, Critical micelle concentration, Cytochrome, Denaturing effect, Detergent extracts, Detergent molecules, Detergent phase, Elution, Elution buffer, Formic acid, Further studies, Fusion protein, General methods, Guanidine, Guanidine hydrochloride, High concentrations, Hplc, Hydrochloric acid, Hydrophilic, Hydrophilic head, Hydrophilic proteins, Hydrophobic, Hydrophobic groups, Hydrophobic interaction, Hydrophobic ligands, Hydrophobic residues, Hydrophobic tail, Important role, Initial stage, Intact protein, Integral membrane protein, Integral membrane proteins, Integral membrane receptor proteins, International symposium, Large integral membrane proteins, Large number, Large volumes, Larger membrane proteins, Less importance, Ligand, Lipid, Lipid bilayer, Liquid chromatography, Magnesium chloride, Major function, Membrane, Membrane protein, Membrane proteins, Methods enzymol, Microbore, Microbore column, Microbore columns, Mild conditions, Mild detergent, Molecular mass, Molecular masses, Monoclonal antibodies, More sites, Multiple peaks, Organic phases, Other membrane proteins, Peak volume, Peptide, Permeation chromatography, Phospholipid molecules, Polyclonal antibodies, Protein, Protein recovery, Protein size, Purification, Receptor, Receptor protein, Receptor proteins, Reference proteins, Respiratory syncytial virus, Salt gradient, Sendai, Sendai virus, Sendai virus membrane proteins, Several times, Sharp peak, Short microbore columns, Sodium chloride, Sodium chloride gradient, Sodium deoxycholate, Sodium phosphate, Solvent concentrations, Solvent peaks, Sulphate, Surface antigen, Total number, Toyo soda, Triton, Viral, Viral membrane proteins, Virol, Vp1fusion protein.
Abstract
Abstract: Biological membranes have as a major function the compartmentation of biological processes in cells and organelles. They consist of a bilayer of phospholipid molecules in which proteins are embedded. These integral membrane proteins, which cross the bilayer once or several times, generally have a higher than average hydrophobicity and tend to aggregate. Detergents are needed to remove integral membrane proteins from the lipid bilayer and they have to be present during further chromatographic purification. Predominantly, four modes of HPLC have been used alone or in combination for the puridication of integral membrane proteins. These are based on differences of proteins in size (size-exclusion chromatography, SEC), electrostatic interaction (ion-exchange chromatography, IEC), bioaffinity (bioaffinity chromatography, BAC) and hydrophobic interaction (reversed-phase chromatography, RPC, and hydrophobic-interaction chromatography, HIC). SEC, IEC, BAC and HIC are used under relatively mild conditions, and buffer systems generally contain a non-ionic detergent. RPC generally has a denaturing effect on the protein and should preferably be used for the purification of integral membrane proteins smaller than 50 kD.
Url:
DOI: 10.1016/0378-4347(87)80010-5
Affiliations:
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Welling</name></author><author><name sortKey="Van Der Zee, Ruurd" sort="Van Der Zee, Ruurd" uniqKey="Van Der Zee R" first="Ruurd" last="Van Der Zee">Ruurd Van Der Zee</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:F4ADEE064004D686805A95E741346A279F6FA696</idno><date when="1987" year="1987">1987</date><idno type="doi">10.1016/0378-4347(87)80010-5</idno><idno type="url">https://api.istex.fr/ark:/67375/6H6-5JT2N1PL-2/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">000466</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">000466</idno><idno type="wicri:Area/Istex/Curation">000433</idno><idno type="wicri:Area/Istex/Checkpoint">000694</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Checkpoint">000694</idno><idno type="wicri:doubleKey">0378-4347:1987:Welling G:column:liquid:chromatography</idno><idno type="wicri:Area/Main/Merge">001D45</idno><idno type="wicri:Area/Main/Curation">001D23</idno><idno type="wicri:Area/Main/Exploration">001D23</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a">Column liquid chromatography of integral 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="1"><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>Laboratorium voor Medische Microbiologie, Rijksuniversiteit Gronigen, Oostersingel 59</wicri:regionArea><wicri:noRegion>Oostersingel 59</wicri:noRegion></affiliation></author><author><name sortKey="Van Der Zee, Ruurd" sort="Van Der Zee, Ruurd" uniqKey="Van Der Zee R" first="Ruurd" last="Van Der Zee">Ruurd Van Der Zee</name><affiliation wicri:level="1"><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>Laboratorium voor Medische Microbiologie, Rijksuniversiteit Gronigen, Oostersingel 59</wicri:regionArea><wicri:noRegion>Oostersingel 59</wicri:noRegion></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="1"><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>Laboratorium voor Medische Microbiologie, Rijksuniversiteit Gronigen, Oostersingel 59</wicri:regionArea><wicri:noRegion>Oostersingel 59</wicri:noRegion></affiliation></author></analytic><monogr></monogr><series><title level="j">Journal of Chromatography B: Biomedical Sciences and Applications</title><title level="j" type="abbrev">CHROLD</title><idno type="ISSN">0378-4347</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1987">1987</date><biblScope unit="volume">418</biblScope><biblScope unit="supplement">C</biblScope><biblScope unit="page" from="223">223</biblScope><biblScope unit="page" to="243">243</biblScope></imprint><idno type="ISSN">0378-4347</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0378-4347</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Amino</term><term>Amino acids</term><term>Ammonium</term><term>Ammonium sulphate</term><term>Ammonium thiocyanate</term><term>Anal</term><term>Anal biochem</term><term>Aqueous phase</term><term>Average protein</term><term>Bilayer</term><term>Bile salts</term><term>Bioaffinity</term><term>Bioaffinity chromatography</term><term>Biochem</term><term>Biol</term><term>Biol chem</term><term>Biological activity</term><term>Biological applications</term><term>Biological processes</term><term>Buffer systems</term><term>Cell biol</term><term>Chem</term><term>Chromatogr</term><term>Chromatographic methodology</term><term>Chromatography</term><term>Coli</term><term>Coli contaminants</term><term>Column length</term><term>Column ligands</term><term>Corona virus</term><term>Critical micelle concentration</term><term>Cytochrome</term><term>Denaturing effect</term><term>Detergent extracts</term><term>Detergent molecules</term><term>Detergent phase</term><term>Elution</term><term>Elution buffer</term><term>Formic acid</term><term>Further studies</term><term>Fusion protein</term><term>General methods</term><term>Guanidine</term><term>Guanidine hydrochloride</term><term>High concentrations</term><term>Hplc</term><term>Hydrochloric acid</term><term>Hydrophilic</term><term>Hydrophilic head</term><term>Hydrophilic proteins</term><term>Hydrophobic</term><term>Hydrophobic groups</term><term>Hydrophobic interaction</term><term>Hydrophobic ligands</term><term>Hydrophobic residues</term><term>Hydrophobic tail</term><term>Important role</term><term>Initial stage</term><term>Intact protein</term><term>Integral membrane protein</term><term>Integral membrane proteins</term><term>Integral membrane receptor proteins</term><term>International symposium</term><term>Large integral membrane proteins</term><term>Large number</term><term>Large volumes</term><term>Larger membrane proteins</term><term>Less importance</term><term>Ligand</term><term>Lipid</term><term>Lipid bilayer</term><term>Liquid chromatography</term><term>Magnesium chloride</term><term>Major function</term><term>Membrane</term><term>Membrane protein</term><term>Membrane proteins</term><term>Methods enzymol</term><term>Microbore</term><term>Microbore column</term><term>Microbore columns</term><term>Mild conditions</term><term>Mild detergent</term><term>Molecular mass</term><term>Molecular masses</term><term>Monoclonal antibodies</term><term>More sites</term><term>Multiple peaks</term><term>Organic phases</term><term>Other membrane proteins</term><term>Peak volume</term><term>Peptide</term><term>Permeation chromatography</term><term>Phospholipid molecules</term><term>Polyclonal antibodies</term><term>Protein</term><term>Protein recovery</term><term>Protein size</term><term>Purification</term><term>Receptor</term><term>Receptor protein</term><term>Receptor proteins</term><term>Reference proteins</term><term>Respiratory syncytial virus</term><term>Salt gradient</term><term>Sendai</term><term>Sendai virus</term><term>Sendai virus membrane proteins</term><term>Several times</term><term>Sharp peak</term><term>Short microbore columns</term><term>Sodium chloride</term><term>Sodium chloride gradient</term><term>Sodium deoxycholate</term><term>Sodium phosphate</term><term>Solvent concentrations</term><term>Solvent peaks</term><term>Sulphate</term><term>Surface antigen</term><term>Total number</term><term>Toyo soda</term><term>Triton</term><term>Viral</term><term>Viral membrane proteins</term><term>Virol</term><term>Vp1fusion protein</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Biological membranes have as a major function the compartmentation of biological processes in cells and organelles. They consist of a bilayer of phospholipid molecules in which proteins are embedded. These integral membrane proteins, which cross the bilayer once or several times, generally have a higher than average hydrophobicity and tend to aggregate. Detergents are needed to remove integral membrane proteins from the lipid bilayer and they have to be present during further chromatographic purification. Predominantly, four modes of HPLC have been used alone or in combination for the puridication of integral membrane proteins. These are based on differences of proteins in size (size-exclusion chromatography, SEC), electrostatic interaction (ion-exchange chromatography, IEC), bioaffinity (bioaffinity chromatography, BAC) and hydrophobic interaction (reversed-phase chromatography, RPC, and hydrophobic-interaction chromatography, HIC). SEC, IEC, BAC and HIC are used under relatively mild conditions, and buffer systems generally contain a non-ionic detergent. RPC generally has a denaturing effect on the protein and should preferably be used for the purification of integral membrane proteins smaller than 50 kD.</div></front></TEI><affiliations><list><country><li>Pays-Bas</li></country></list><tree><country name="Pays-Bas"><noRegion><name sortKey="Welling, Gjalt W" sort="Welling, Gjalt W" uniqKey="Welling G" first="Gjalt W." last="Welling">Gjalt W. Welling</name></noRegion><name sortKey="Van Der Zee, Ruurd" sort="Van Der Zee, Ruurd" uniqKey="Van Der Zee R" first="Ruurd" last="Van Der Zee">Ruurd Van Der Zee</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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