Plasma membrane receptor for beta-lactoglobulin and retinol-binding protein in murine hybridomas
The aim of the present work was to study the binding of [125I]‐BLGA (β‐lactoglobulin variant A) to the plasma membrane fraction of hybrid cells. This binding increased as a function of time with on‐rate and off‐rate constant at 4.47 ± 0.18× 106 M−1 min−1 and 0.17 ± 0.07 min−1, respectively (n = 3)....
Gespeichert in:
| Veröffentlicht in: | BioFactors (Oxford) 1998, Vol.7 (4), p.287-298 |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 298 |
|---|---|
| container_issue | 4 |
| container_start_page | 287 |
| container_title | BioFactors (Oxford) |
| container_volume | 7 |
| creator | Mansouri, Abdelali Guéant, Jean-Louis Capiaumont, Josette Pelosi, Paolo Nabet, Pierre Haertlé, Thomas |
| description | The aim of the present work was to study the binding of [125I]‐BLGA (β‐lactoglobulin variant A) to the plasma membrane fraction of hybrid cells. This binding increased as a function of time with on‐rate and off‐rate constant at 4.47 ± 0.18× 106 M−1 min−1 and 0.17 ± 0.07 min−1, respectively (n = 3). The saturation study showed a single binding site type corresponding to a Kd at 8.26 ± 2.98 nM and 14.02 ± 2.61× 1012 sites per mg of the plasma membrane protein (n = 3). Competitive of binding BLGA was observed with BLGA, complexed with retinol and also with RBP (retinol‐binding protein). Gel filtration of [125I]‐BLGA incubated with Triton X‐100 solubilized membrane showed the formation of a ligand‐receptor complex. Cross‐linking of the tracer to plasma membrane showed a complex with a Mr at 69 kDa, suggesting a receptor M_r of 51 kDa, as seen by autoradiography of SDS‐PAGE. |
| doi_str_mv | 10.1002/biof.5520070401 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_80012109</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>80012109</sourcerecordid><originalsourceid>FETCH-LOGICAL-c3821-f5d5203f92957a26a347a959d48c892f4f1f9628e18369b2a864ef9c973db5f43</originalsourceid><addsrcrecordid>eNqFkEtPxCAAhInR6Po4ezLpyVuVR0shntyNr2SjxucRoQVFaVmhje6_F7MbjScTCIeZ-cIMALsIHiAI8aGy3hyUJYawggVEK2CEWIVzBhlaBSPIS5TTgpANsBnjK4SIwIKtg3VOKSWoGoGnaydjK7NWtyrITmdB13rW-5CZdJXuZe5k3ftn59XgbJfJrkme3nbe5cp2je2es1nwvU5aOu0QbKK8zFWwjW9l3AZrRrqod5bvFrg_PbmbnOfTq7OLyfE0rwnDKDdlk0oQwzEvK4mpJEUlecmbgtWMY1MYZDjFTCNGKFdYMlpow2tekUaVpiBbYH_BTZ95H3TsRWtjrZ1LpfwQBUvlMYI8GQ8Xxjr4GIM2YhZsK8NcICi-NxXfm4rfTVNib4keVKubH_9yxKQfLfQP6_T8P5wYX1yd_qHni7SNvf78ScvwJmhFqlI8Xp6JMR5jNn24EbfkC_tVk4g</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>80012109</pqid></control><display><type>article</type><title>Plasma membrane receptor for beta-lactoglobulin and retinol-binding protein in murine hybridomas</title><source>MEDLINE</source><source>Access via Wiley Online Library</source><creator>Mansouri, Abdelali ; Guéant, Jean-Louis ; Capiaumont, Josette ; Pelosi, Paolo ; Nabet, Pierre ; Haertlé, Thomas</creator><creatorcontrib>Mansouri, Abdelali ; Guéant, Jean-Louis ; Capiaumont, Josette ; Pelosi, Paolo ; Nabet, Pierre ; Haertlé, Thomas</creatorcontrib><description>The aim of the present work was to study the binding of [125I]‐BLGA (β‐lactoglobulin variant A) to the plasma membrane fraction of hybrid cells. This binding increased as a function of time with on‐rate and off‐rate constant at 4.47 ± 0.18× 106 M−1 min−1 and 0.17 ± 0.07 min−1, respectively (n = 3). The saturation study showed a single binding site type corresponding to a Kd at 8.26 ± 2.98 nM and 14.02 ± 2.61× 1012 sites per mg of the plasma membrane protein (n = 3). Competitive of binding BLGA was observed with BLGA, complexed with retinol and also with RBP (retinol‐binding protein). Gel filtration of [125I]‐BLGA incubated with Triton X‐100 solubilized membrane showed the formation of a ligand‐receptor complex. Cross‐linking of the tracer to plasma membrane showed a complex with a Mr at 69 kDa, suggesting a receptor M_r of 51 kDa, as seen by autoradiography of SDS‐PAGE.</description><identifier>ISSN: 0951-6433</identifier><identifier>EISSN: 1872-8081</identifier><identifier>DOI: 10.1002/biof.5520070401</identifier><identifier>PMID: 9666317</identifier><language>eng</language><publisher>Amsterdam: IOS Press</publisher><subject>Animals ; Autoradiography ; Binding, Competitive ; Cell Membrane - metabolism ; Chromatography, Gel ; Cross-Linking Reagents ; Electrophoresis, Polyacrylamide Gel ; hybridoma cells ; Hybridomas - metabolism ; Iodine Radioisotopes ; Lactoglobulins - metabolism ; Mice ; Octoxynol ; receptor ; Receptors, Cell Surface - metabolism ; retinol ; retinol-binding protein ; Retinol-Binding Proteins - metabolism ; Retinol-Binding Proteins, Plasma ; Solubility ; Vitamin A - metabolism ; β-lactoglobulin</subject><ispartof>BioFactors (Oxford), 1998, Vol.7 (4), p.287-298</ispartof><rights>Copyright © 1998 International Union of Biochemistry and Molecular Biology, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3821-f5d5203f92957a26a347a959d48c892f4f1f9628e18369b2a864ef9c973db5f43</citedby><cites>FETCH-LOGICAL-c3821-f5d5203f92957a26a347a959d48c892f4f1f9628e18369b2a864ef9c973db5f43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fbiof.5520070401$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fbiof.5520070401$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,4024,27923,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9666317$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mansouri, Abdelali</creatorcontrib><creatorcontrib>Guéant, Jean-Louis</creatorcontrib><creatorcontrib>Capiaumont, Josette</creatorcontrib><creatorcontrib>Pelosi, Paolo</creatorcontrib><creatorcontrib>Nabet, Pierre</creatorcontrib><creatorcontrib>Haertlé, Thomas</creatorcontrib><title>Plasma membrane receptor for beta-lactoglobulin and retinol-binding protein in murine hybridomas</title><title>BioFactors (Oxford)</title><addtitle>BioFactors</addtitle><description>The aim of the present work was to study the binding of [125I]‐BLGA (β‐lactoglobulin variant A) to the plasma membrane fraction of hybrid cells. This binding increased as a function of time with on‐rate and off‐rate constant at 4.47 ± 0.18× 106 M−1 min−1 and 0.17 ± 0.07 min−1, respectively (n = 3). The saturation study showed a single binding site type corresponding to a Kd at 8.26 ± 2.98 nM and 14.02 ± 2.61× 1012 sites per mg of the plasma membrane protein (n = 3). Competitive of binding BLGA was observed with BLGA, complexed with retinol and also with RBP (retinol‐binding protein). Gel filtration of [125I]‐BLGA incubated with Triton X‐100 solubilized membrane showed the formation of a ligand‐receptor complex. Cross‐linking of the tracer to plasma membrane showed a complex with a Mr at 69 kDa, suggesting a receptor M_r of 51 kDa, as seen by autoradiography of SDS‐PAGE.</description><subject>Animals</subject><subject>Autoradiography</subject><subject>Binding, Competitive</subject><subject>Cell Membrane - metabolism</subject><subject>Chromatography, Gel</subject><subject>Cross-Linking Reagents</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>hybridoma cells</subject><subject>Hybridomas - metabolism</subject><subject>Iodine Radioisotopes</subject><subject>Lactoglobulins - metabolism</subject><subject>Mice</subject><subject>Octoxynol</subject><subject>receptor</subject><subject>Receptors, Cell Surface - metabolism</subject><subject>retinol</subject><subject>retinol-binding protein</subject><subject>Retinol-Binding Proteins - metabolism</subject><subject>Retinol-Binding Proteins, Plasma</subject><subject>Solubility</subject><subject>Vitamin A - metabolism</subject><subject>β-lactoglobulin</subject><issn>0951-6433</issn><issn>1872-8081</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkEtPxCAAhInR6Po4ezLpyVuVR0shntyNr2SjxucRoQVFaVmhje6_F7MbjScTCIeZ-cIMALsIHiAI8aGy3hyUJYawggVEK2CEWIVzBhlaBSPIS5TTgpANsBnjK4SIwIKtg3VOKSWoGoGnaydjK7NWtyrITmdB13rW-5CZdJXuZe5k3ftn59XgbJfJrkme3nbe5cp2je2es1nwvU5aOu0QbKK8zFWwjW9l3AZrRrqod5bvFrg_PbmbnOfTq7OLyfE0rwnDKDdlk0oQwzEvK4mpJEUlecmbgtWMY1MYZDjFTCNGKFdYMlpow2tekUaVpiBbYH_BTZ95H3TsRWtjrZ1LpfwQBUvlMYI8GQ8Xxjr4GIM2YhZsK8NcICi-NxXfm4rfTVNib4keVKubH_9yxKQfLfQP6_T8P5wYX1yd_qHni7SNvf78ScvwJmhFqlI8Xp6JMR5jNn24EbfkC_tVk4g</recordid><startdate>1998</startdate><enddate>1998</enddate><creator>Mansouri, Abdelali</creator><creator>Guéant, Jean-Louis</creator><creator>Capiaumont, Josette</creator><creator>Pelosi, Paolo</creator><creator>Nabet, Pierre</creator><creator>Haertlé, Thomas</creator><general>IOS Press</general><scope>BSCLL</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>1998</creationdate><title>Plasma membrane receptor for beta-lactoglobulin and retinol-binding protein in murine hybridomas</title><author>Mansouri, Abdelali ; Guéant, Jean-Louis ; Capiaumont, Josette ; Pelosi, Paolo ; Nabet, Pierre ; Haertlé, Thomas</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3821-f5d5203f92957a26a347a959d48c892f4f1f9628e18369b2a864ef9c973db5f43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Animals</topic><topic>Autoradiography</topic><topic>Binding, Competitive</topic><topic>Cell Membrane - metabolism</topic><topic>Chromatography, Gel</topic><topic>Cross-Linking Reagents</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>hybridoma cells</topic><topic>Hybridomas - metabolism</topic><topic>Iodine Radioisotopes</topic><topic>Lactoglobulins - metabolism</topic><topic>Mice</topic><topic>Octoxynol</topic><topic>receptor</topic><topic>Receptors, Cell Surface - metabolism</topic><topic>retinol</topic><topic>retinol-binding protein</topic><topic>Retinol-Binding Proteins - metabolism</topic><topic>Retinol-Binding Proteins, Plasma</topic><topic>Solubility</topic><topic>Vitamin A - metabolism</topic><topic>β-lactoglobulin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mansouri, Abdelali</creatorcontrib><creatorcontrib>Guéant, Jean-Louis</creatorcontrib><creatorcontrib>Capiaumont, Josette</creatorcontrib><creatorcontrib>Pelosi, Paolo</creatorcontrib><creatorcontrib>Nabet, Pierre</creatorcontrib><creatorcontrib>Haertlé, Thomas</creatorcontrib><collection>Istex</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>BioFactors (Oxford)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mansouri, Abdelali</au><au>Guéant, Jean-Louis</au><au>Capiaumont, Josette</au><au>Pelosi, Paolo</au><au>Nabet, Pierre</au><au>Haertlé, Thomas</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Plasma membrane receptor for beta-lactoglobulin and retinol-binding protein in murine hybridomas</atitle><jtitle>BioFactors (Oxford)</jtitle><addtitle>BioFactors</addtitle><date>1998</date><risdate>1998</risdate><volume>7</volume><issue>4</issue><spage>287</spage><epage>298</epage><pages>287-298</pages><issn>0951-6433</issn><eissn>1872-8081</eissn><abstract>The aim of the present work was to study the binding of [125I]‐BLGA (β‐lactoglobulin variant A) to the plasma membrane fraction of hybrid cells. This binding increased as a function of time with on‐rate and off‐rate constant at 4.47 ± 0.18× 106 M−1 min−1 and 0.17 ± 0.07 min−1, respectively (n = 3). The saturation study showed a single binding site type corresponding to a Kd at 8.26 ± 2.98 nM and 14.02 ± 2.61× 1012 sites per mg of the plasma membrane protein (n = 3). Competitive of binding BLGA was observed with BLGA, complexed with retinol and also with RBP (retinol‐binding protein). Gel filtration of [125I]‐BLGA incubated with Triton X‐100 solubilized membrane showed the formation of a ligand‐receptor complex. Cross‐linking of the tracer to plasma membrane showed a complex with a Mr at 69 kDa, suggesting a receptor M_r of 51 kDa, as seen by autoradiography of SDS‐PAGE.</abstract><cop>Amsterdam</cop><pub>IOS Press</pub><pmid>9666317</pmid><doi>10.1002/biof.5520070401</doi><tpages>12</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0951-6433 |
| ispartof | BioFactors (Oxford), 1998, Vol.7 (4), p.287-298 |
| issn | 0951-6433 1872-8081 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_80012109 |
| source | MEDLINE; Access via Wiley Online Library |
| subjects | Animals Autoradiography Binding, Competitive Cell Membrane - metabolism Chromatography, Gel Cross-Linking Reagents Electrophoresis, Polyacrylamide Gel hybridoma cells Hybridomas - metabolism Iodine Radioisotopes Lactoglobulins - metabolism Mice Octoxynol receptor Receptors, Cell Surface - metabolism retinol retinol-binding protein Retinol-Binding Proteins - metabolism Retinol-Binding Proteins, Plasma Solubility Vitamin A - metabolism β-lactoglobulin |
| title | Plasma membrane receptor for beta-lactoglobulin and retinol-binding protein in murine hybridomas |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-02T12%3A12%3A21IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Plasma%20membrane%20receptor%20for%20beta-lactoglobulin%20and%20retinol-binding%20protein%20in%20murine%20hybridomas&rft.jtitle=BioFactors%20(Oxford)&rft.au=Mansouri,%20Abdelali&rft.date=1998&rft.volume=7&rft.issue=4&rft.spage=287&rft.epage=298&rft.pages=287-298&rft.issn=0951-6433&rft.eissn=1872-8081&rft_id=info:doi/10.1002/biof.5520070401&rft_dat=%3Cproquest_cross%3E80012109%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=80012109&rft_id=info:pmid/9666317&rfr_iscdi=true |