Isolation and purification of the Rh(D) blood group receptor component from human erythrocyte membrane
The Rh(D) antigen of human red blood cell membranes has been isolated as a homogeneous immunologically intact component. The method of preparation was as follows: Red cell membranes were prepared free of hemoglobin and components were solubilized using ethylenediaminetetraacetic acid (EDTA) followed...
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| Veröffentlicht in: | Clinica chimica acta 1975-04, Vol.60 (1), p.33-43 |
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| container_title | Clinica chimica acta |
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| creator | Abraham, C.V. Bakerman, S. |
| description | The Rh(D) antigen of human red blood cell membranes has been isolated as a homogeneous immunologically intact component. The method of preparation was as follows: Red cell membranes were prepared free of hemoglobin and components were solubilized using ethylenediaminetetraacetic acid (EDTA) followed by sodium chloride. Diaflo® ultrafilter membranes were used to separate solubilized membrane components into different molecular weight classes. The Rh(D) activity was demonstrated in the molecular weight class between 10 000 and 20 000. This fraction, which had six components by disc gel electrophoresis, was further purified by isoelectric focusing on a pH gradient of 3 to 10, followed by a pH gradient of 5 to 8. The Rh(D) antigen was eluted as a single component, migrated as a discrete band on disc gel electrophoresis, and inhibited the agglutination of anti-Rh(D) antibody. When the Rh(D) antigen was injected into guinea pigs, a high titer of anti-Rh(D) antibody was obtained. |
| doi_str_mv | 10.1016/0009-8981(75)90177-1 |
| format | Article |
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The method of preparation was as follows: Red cell membranes were prepared free of hemoglobin and components were solubilized using ethylenediaminetetraacetic acid (EDTA) followed by sodium chloride. Diaflo® ultrafilter membranes were used to separate solubilized membrane components into different molecular weight classes. The Rh(D) activity was demonstrated in the molecular weight class between 10 000 and 20 000. This fraction, which had six components by disc gel electrophoresis, was further purified by isoelectric focusing on a pH gradient of 3 to 10, followed by a pH gradient of 5 to 8. The Rh(D) antigen was eluted as a single component, migrated as a discrete band on disc gel electrophoresis, and inhibited the agglutination of anti-Rh(D) antibody. When the Rh(D) antigen was injected into guinea pigs, a high titer of anti-Rh(D) antibody was obtained.</description><identifier>ISSN: 0009-8981</identifier><identifier>EISSN: 1873-3492</identifier><identifier>DOI: 10.1016/0009-8981(75)90177-1</identifier><identifier>PMID: 805006</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Animals ; Antigens - isolation & purification ; Binding Sites, Antibody ; Cell Membrane - analysis ; Edetic Acid ; Electrophoresis, Disc ; Electrophoresis, Polyacrylamide Gel ; Erythrocytes - analysis ; Guinea Pigs - immunology ; Hemagglutination Inhibition Tests ; Humans ; Isoelectric Focusing ; Molecular Weight ; Protein Binding ; Rh-Hr Blood-Group System ; Solubility ; Ultrafiltration</subject><ispartof>Clinica chimica acta, 1975-04, Vol.60 (1), p.33-43</ispartof><rights>1975</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c402t-fdf3800ef89c461e9663cd4fdc6a0a5e63e260676171189943954f508ef572c73</citedby><cites>FETCH-LOGICAL-c402t-fdf3800ef89c461e9663cd4fdc6a0a5e63e260676171189943954f508ef572c73</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0009898175901771$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/805006$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Abraham, C.V.</creatorcontrib><creatorcontrib>Bakerman, S.</creatorcontrib><title>Isolation and purification of the Rh(D) blood group receptor component from human erythrocyte membrane</title><title>Clinica chimica acta</title><addtitle>Clin Chim Acta</addtitle><description>The Rh(D) antigen of human red blood cell membranes has been isolated as a homogeneous immunologically intact component. The method of preparation was as follows: Red cell membranes were prepared free of hemoglobin and components were solubilized using ethylenediaminetetraacetic acid (EDTA) followed by sodium chloride. Diaflo® ultrafilter membranes were used to separate solubilized membrane components into different molecular weight classes. The Rh(D) activity was demonstrated in the molecular weight class between 10 000 and 20 000. This fraction, which had six components by disc gel electrophoresis, was further purified by isoelectric focusing on a pH gradient of 3 to 10, followed by a pH gradient of 5 to 8. The Rh(D) antigen was eluted as a single component, migrated as a discrete band on disc gel electrophoresis, and inhibited the agglutination of anti-Rh(D) antibody. When the Rh(D) antigen was injected into guinea pigs, a high titer of anti-Rh(D) antibody was obtained.</description><subject>Animals</subject><subject>Antigens - isolation & purification</subject><subject>Binding Sites, Antibody</subject><subject>Cell Membrane - analysis</subject><subject>Edetic Acid</subject><subject>Electrophoresis, Disc</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Erythrocytes - analysis</subject><subject>Guinea Pigs - immunology</subject><subject>Hemagglutination Inhibition Tests</subject><subject>Humans</subject><subject>Isoelectric Focusing</subject><subject>Molecular Weight</subject><subject>Protein Binding</subject><subject>Rh-Hr Blood-Group System</subject><subject>Solubility</subject><subject>Ultrafiltration</subject><issn>0009-8981</issn><issn>1873-3492</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1975</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1r3DAQhkVJm2zT_oMcdArJwcnIH_q4BEKaj4WFQGnPwiuPuiq25UhyYP997XrZY07DzPvOy8xDyAWDGwaM3wKAyqSS7EpU1wqYEBn7RFZMiiIrSpWfkNXRcka-xvh3akvg7JR8kVAB8BWx6-jbOjnf07pv6DAGZ51ZBt7StEP6c3f145puW-8b-if4caABDQ7JB2p8N_ge-0Rt8B3djV3dUwz7tAve7BPSDrttqHv8Rj7buo34_VDPye-nx18PL9nm9Xn9cL_JTAl5ymxjCwmAVipTcoaK88I0pW0Mr6GukBeYc-CCM8GYVKosVFXaCiTaSuRGFOfkcskdgn8bMSbduWiwbacb_Bi1zGXOC8EmY7kYTfAxBrR6CK6rw14z0DNdPaPTMzotKv2frp7XLg7547bD5ri04Jzku0XG6cd3h0FH47A32LiJWdKNdx_n_wOTRYlq</recordid><startdate>19750402</startdate><enddate>19750402</enddate><creator>Abraham, C.V.</creator><creator>Bakerman, S.</creator><general>Elsevier B.V</general><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>19750402</creationdate><title>Isolation and purification of the Rh(D) blood group receptor component from human erythrocyte membrane</title><author>Abraham, C.V. ; Bakerman, S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c402t-fdf3800ef89c461e9663cd4fdc6a0a5e63e260676171189943954f508ef572c73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1975</creationdate><topic>Animals</topic><topic>Antigens - isolation & purification</topic><topic>Binding Sites, Antibody</topic><topic>Cell Membrane - analysis</topic><topic>Edetic Acid</topic><topic>Electrophoresis, Disc</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Erythrocytes - analysis</topic><topic>Guinea Pigs - immunology</topic><topic>Hemagglutination Inhibition Tests</topic><topic>Humans</topic><topic>Isoelectric Focusing</topic><topic>Molecular Weight</topic><topic>Protein Binding</topic><topic>Rh-Hr Blood-Group System</topic><topic>Solubility</topic><topic>Ultrafiltration</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Abraham, C.V.</creatorcontrib><creatorcontrib>Bakerman, S.</creatorcontrib><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>Clinica chimica acta</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Abraham, C.V.</au><au>Bakerman, S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Isolation and purification of the Rh(D) blood group receptor component from human erythrocyte membrane</atitle><jtitle>Clinica chimica acta</jtitle><addtitle>Clin Chim Acta</addtitle><date>1975-04-02</date><risdate>1975</risdate><volume>60</volume><issue>1</issue><spage>33</spage><epage>43</epage><pages>33-43</pages><issn>0009-8981</issn><eissn>1873-3492</eissn><abstract>The Rh(D) antigen of human red blood cell membranes has been isolated as a homogeneous immunologically intact component. The method of preparation was as follows: Red cell membranes were prepared free of hemoglobin and components were solubilized using ethylenediaminetetraacetic acid (EDTA) followed by sodium chloride. Diaflo® ultrafilter membranes were used to separate solubilized membrane components into different molecular weight classes. The Rh(D) activity was demonstrated in the molecular weight class between 10 000 and 20 000. This fraction, which had six components by disc gel electrophoresis, was further purified by isoelectric focusing on a pH gradient of 3 to 10, followed by a pH gradient of 5 to 8. The Rh(D) antigen was eluted as a single component, migrated as a discrete band on disc gel electrophoresis, and inhibited the agglutination of anti-Rh(D) antibody. When the Rh(D) antigen was injected into guinea pigs, a high titer of anti-Rh(D) antibody was obtained.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>805006</pmid><doi>10.1016/0009-8981(75)90177-1</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Clinica chimica acta, 1975-04, Vol.60 (1), p.33-43 |
| issn | 0009-8981 1873-3492 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Animals Antigens - isolation & purification Binding Sites, Antibody Cell Membrane - analysis Edetic Acid Electrophoresis, Disc Electrophoresis, Polyacrylamide Gel Erythrocytes - analysis Guinea Pigs - immunology Hemagglutination Inhibition Tests Humans Isoelectric Focusing Molecular Weight Protein Binding Rh-Hr Blood-Group System Solubility Ultrafiltration |
| title | Isolation and purification of the Rh(D) blood group receptor component from human erythrocyte membrane |
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