Extraction and purification of the chief glycoprotein of the erythrocyte membrane
The major glycoprotein of the human erythrocyte membrane has been released from ghosts, by the non-ionic detergent Tween 20 at pH 8,5 and at low ionic strength and further purified by successive passages through columns of DEAE Sephadex at pH 6,8 and CM Sephadex at pH 5 or by hydroxyapatite chromato...
Gespeichert in:
| Veröffentlicht in: | Revue française de transfusion et immunohématologie 1979-09, Vol.22 (4), p.329 |
|---|---|
| Hauptverfasser: | , |
| Format: | Artikel |
| Sprache: | fre |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | |
|---|---|
| container_issue | 4 |
| container_start_page | 329 |
| container_title | Revue française de transfusion et immunohématologie |
| container_volume | 22 |
| creator | Le Bec, A Mayer, S |
| description | The major glycoprotein of the human erythrocyte membrane has been released from ghosts, by the non-ionic detergent Tween 20 at pH 8,5 and at low ionic strength and further purified by successive passages through columns of DEAE Sephadex at pH 6,8 and CM Sephadex at pH 5 or by hydroxyapatite chromatography at pH 6,8. The purified glycoprotein thus obtained represents about 1 % of the membrane proteins, and shows two major bands upon polyacrylamide gel electrophoresis. These bands designed as PAS 1 and PAS 2 are the dimer and the monomer of the glycoprotein. Several other minor bands can also appear on SDS gels, according to experimental conditions of solubilization and purification and are probably oligomers of PAS 1 and PAS 2. This glycoprotein possess inhibitory activity against various phytohemagglutinins. |
| format | Article |
| fullrecord | <record><control><sourceid>pubmed</sourceid><recordid>TN_cdi_pubmed_primary_556211</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>556211</sourcerecordid><originalsourceid>FETCH-pubmed_primary_5562113</originalsourceid><addsrcrecordid>eNqFjrsKwjAUQDP4qo8_cMgPFBJjfMxScRXcS5re2EjThNsUzN8LKq5OB85ZzohkTIhDvpVCzsi87x-Mif2RsymZSLnbcJ6Ra_GMqHS0vqOqq2kY0Bqr1Vt4Q2MDVDcWDL23SfuAPoL9FcAUG_Q6RaAOXIWqgyUZG9X2sPpyQdbn4na65GGoHNRlQOsUpvJzIP7kFxlWPDA</addsrcrecordid><sourcetype>Index Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>Extraction and purification of the chief glycoprotein of the erythrocyte membrane</title><source>MEDLINE</source><source>Alma/SFX Local Collection</source><creator>Le Bec, A ; Mayer, S</creator><creatorcontrib>Le Bec, A ; Mayer, S</creatorcontrib><description>The major glycoprotein of the human erythrocyte membrane has been released from ghosts, by the non-ionic detergent Tween 20 at pH 8,5 and at low ionic strength and further purified by successive passages through columns of DEAE Sephadex at pH 6,8 and CM Sephadex at pH 5 or by hydroxyapatite chromatography at pH 6,8. The purified glycoprotein thus obtained represents about 1 % of the membrane proteins, and shows two major bands upon polyacrylamide gel electrophoresis. These bands designed as PAS 1 and PAS 2 are the dimer and the monomer of the glycoprotein. Several other minor bands can also appear on SDS gels, according to experimental conditions of solubilization and purification and are probably oligomers of PAS 1 and PAS 2. This glycoprotein possess inhibitory activity against various phytohemagglutinins.</description><identifier>ISSN: 0338-4535</identifier><identifier>PMID: 556211</identifier><language>fre</language><publisher>France</publisher><subject>Carbohydrates ; Chromatography ; Chromatography, Ion Exchange ; Erythrocyte Membrane - analysis ; Erythrocytes - analysis ; Glycophorin - isolation & purification ; Glycoproteins - isolation & purification ; Hemagglutination Tests ; Hydroxyapatites ; Lectins - pharmacology</subject><ispartof>Revue française de transfusion et immunohématologie, 1979-09, Vol.22 (4), p.329</ispartof><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/556211$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Le Bec, A</creatorcontrib><creatorcontrib>Mayer, S</creatorcontrib><title>Extraction and purification of the chief glycoprotein of the erythrocyte membrane</title><title>Revue française de transfusion et immunohématologie</title><addtitle>Rev Fr Transfus Immunohematol</addtitle><description>The major glycoprotein of the human erythrocyte membrane has been released from ghosts, by the non-ionic detergent Tween 20 at pH 8,5 and at low ionic strength and further purified by successive passages through columns of DEAE Sephadex at pH 6,8 and CM Sephadex at pH 5 or by hydroxyapatite chromatography at pH 6,8. The purified glycoprotein thus obtained represents about 1 % of the membrane proteins, and shows two major bands upon polyacrylamide gel electrophoresis. These bands designed as PAS 1 and PAS 2 are the dimer and the monomer of the glycoprotein. Several other minor bands can also appear on SDS gels, according to experimental conditions of solubilization and purification and are probably oligomers of PAS 1 and PAS 2. This glycoprotein possess inhibitory activity against various phytohemagglutinins.</description><subject>Carbohydrates</subject><subject>Chromatography</subject><subject>Chromatography, Ion Exchange</subject><subject>Erythrocyte Membrane - analysis</subject><subject>Erythrocytes - analysis</subject><subject>Glycophorin - isolation & purification</subject><subject>Glycoproteins - isolation & purification</subject><subject>Hemagglutination Tests</subject><subject>Hydroxyapatites</subject><subject>Lectins - pharmacology</subject><issn>0338-4535</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1979</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFjrsKwjAUQDP4qo8_cMgPFBJjfMxScRXcS5re2EjThNsUzN8LKq5OB85ZzohkTIhDvpVCzsi87x-Mif2RsymZSLnbcJ6Ra_GMqHS0vqOqq2kY0Bqr1Vt4Q2MDVDcWDL23SfuAPoL9FcAUG_Q6RaAOXIWqgyUZG9X2sPpyQdbn4na65GGoHNRlQOsUpvJzIP7kFxlWPDA</recordid><startdate>197909</startdate><enddate>197909</enddate><creator>Le Bec, A</creator><creator>Mayer, S</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope></search><sort><creationdate>197909</creationdate><title>Extraction and purification of the chief glycoprotein of the erythrocyte membrane</title><author>Le Bec, A ; Mayer, S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-pubmed_primary_5562113</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>fre</language><creationdate>1979</creationdate><topic>Carbohydrates</topic><topic>Chromatography</topic><topic>Chromatography, Ion Exchange</topic><topic>Erythrocyte Membrane - analysis</topic><topic>Erythrocytes - analysis</topic><topic>Glycophorin - isolation & purification</topic><topic>Glycoproteins - isolation & purification</topic><topic>Hemagglutination Tests</topic><topic>Hydroxyapatites</topic><topic>Lectins - pharmacology</topic><toplevel>online_resources</toplevel><creatorcontrib>Le Bec, A</creatorcontrib><creatorcontrib>Mayer, S</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><jtitle>Revue française de transfusion et immunohématologie</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Le Bec, A</au><au>Mayer, S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Extraction and purification of the chief glycoprotein of the erythrocyte membrane</atitle><jtitle>Revue française de transfusion et immunohématologie</jtitle><addtitle>Rev Fr Transfus Immunohematol</addtitle><date>1979-09</date><risdate>1979</risdate><volume>22</volume><issue>4</issue><spage>329</spage><pages>329-</pages><issn>0338-4535</issn><abstract>The major glycoprotein of the human erythrocyte membrane has been released from ghosts, by the non-ionic detergent Tween 20 at pH 8,5 and at low ionic strength and further purified by successive passages through columns of DEAE Sephadex at pH 6,8 and CM Sephadex at pH 5 or by hydroxyapatite chromatography at pH 6,8. The purified glycoprotein thus obtained represents about 1 % of the membrane proteins, and shows two major bands upon polyacrylamide gel electrophoresis. These bands designed as PAS 1 and PAS 2 are the dimer and the monomer of the glycoprotein. Several other minor bands can also appear on SDS gels, according to experimental conditions of solubilization and purification and are probably oligomers of PAS 1 and PAS 2. This glycoprotein possess inhibitory activity against various phytohemagglutinins.</abstract><cop>France</cop><pmid>556211</pmid></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0338-4535 |
| ispartof | Revue française de transfusion et immunohématologie, 1979-09, Vol.22 (4), p.329 |
| issn | 0338-4535 |
| language | fre |
| recordid | cdi_pubmed_primary_556211 |
| source | MEDLINE; Alma/SFX Local Collection |
| subjects | Carbohydrates Chromatography Chromatography, Ion Exchange Erythrocyte Membrane - analysis Erythrocytes - analysis Glycophorin - isolation & purification Glycoproteins - isolation & purification Hemagglutination Tests Hydroxyapatites Lectins - pharmacology |
| title | Extraction and purification of the chief glycoprotein of the erythrocyte membrane |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-24T14%3A29%3A31IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-pubmed&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Extraction%20and%20purification%20of%20the%20chief%20glycoprotein%20of%20the%20erythrocyte%20membrane&rft.jtitle=Revue%20fran%C3%A7aise%20de%20transfusion%20et%20immunoh%C3%A9matologie&rft.au=Le%20Bec,%20A&rft.date=1979-09&rft.volume=22&rft.issue=4&rft.spage=329&rft.pages=329-&rft.issn=0338-4535&rft_id=info:doi/&rft_dat=%3Cpubmed%3E556211%3C/pubmed%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_id=info:pmid/556211&rfr_iscdi=true |