Electrophoretic Polymorphism of Human C4 is Due to Charge Differences in the α‐Chain, Presumably in the C4d Fragment
Various common C4 gene products were isolated from serum by immunoprecipitation. After reduction the C4 α‐, β‐, and γ‐polypeptide chains were studied by two‐dimensional electrophoresis. Isoelectrofocusing was performed in the first dimension and sodium dodecyl sulphate polyacrylamide gradient gel el...
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Veröffentlicht in: | Scandinavian journal of immunology 1981-09, Vol.14 (3), p.303-307 |
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description | Various common C4 gene products were isolated from serum by immunoprecipitation. After reduction the C4 α‐, β‐, and γ‐polypeptide chains were studied by two‐dimensional electrophoresis. Isoelectrofocusing was performed in the first dimension and sodium dodecyl sulphate polyacrylamide gradient gel electrophoresis in the second. The charge differences behind the electrophoretic C4 polymorphism were shown to reside in the 95,000‐u(atmic mass units) α‐chain. Charge variation closely mirroring the α‐chain differences were also found in a 49,000‐u fragment of the α‐chain, most probably C4d. The basic β‐chain could not be studied in detail, but no differences were observed with regard to molecular weight or charge of the γ‐chains of the different C4 gene products. |
doi_str_mv | 10.1111/j.1365-3083.1981.tb00568.x |
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After reduction the C4 α‐, β‐, and γ‐polypeptide chains were studied by two‐dimensional electrophoresis. Isoelectrofocusing was performed in the first dimension and sodium dodecyl sulphate polyacrylamide gradient gel electrophoresis in the second. The charge differences behind the electrophoretic C4 polymorphism were shown to reside in the 95,000‐u(atmic mass units) α‐chain. Charge variation closely mirroring the α‐chain differences were also found in a 49,000‐u fragment of the α‐chain, most probably C4d. The basic β‐chain could not be studied in detail, but no differences were observed with regard to molecular weight or charge of the γ‐chains of the different C4 gene products.</description><identifier>ISSN: 0300-9475</identifier><identifier>EISSN: 1365-3083</identifier><identifier>DOI: 10.1111/j.1365-3083.1981.tb00568.x</identifier><identifier>PMID: 7330601</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Complement C4 - genetics ; Complement C4 - isolation & purification ; Electrophoresis ; Electrophoresis, Polyacrylamide Gel ; Humans ; Isoelectric Focusing ; Molecular Weight ; Peptide Fragments - isolation & purification ; Polymorphism, Genetic</subject><ispartof>Scandinavian journal of immunology, 1981-09, Vol.14 (3), p.303-307</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3153-15bdce2b1fb5f0989698d46e97fa2472b45d641830a0225091935bee01106b573</citedby><cites>FETCH-LOGICAL-c3153-15bdce2b1fb5f0989698d46e97fa2472b45d641830a0225091935bee01106b573</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1365-3083.1981.tb00568.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1365-3083.1981.tb00568.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7330601$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>MEVÅG, B.</creatorcontrib><creatorcontrib>OLAISEN, B.</creatorcontrib><creatorcontrib>TEISBERG, P.</creatorcontrib><title>Electrophoretic Polymorphism of Human C4 is Due to Charge Differences in the α‐Chain, Presumably in the C4d Fragment</title><title>Scandinavian journal of immunology</title><addtitle>Scand J Immunol</addtitle><description>Various common C4 gene products were isolated from serum by immunoprecipitation. After reduction the C4 α‐, β‐, and γ‐polypeptide chains were studied by two‐dimensional electrophoresis. Isoelectrofocusing was performed in the first dimension and sodium dodecyl sulphate polyacrylamide gradient gel electrophoresis in the second. The charge differences behind the electrophoretic C4 polymorphism were shown to reside in the 95,000‐u(atmic mass units) α‐chain. Charge variation closely mirroring the α‐chain differences were also found in a 49,000‐u fragment of the α‐chain, most probably C4d. The basic β‐chain could not be studied in detail, but no differences were observed with regard to molecular weight or charge of the γ‐chains of the different C4 gene products.</description><subject>Complement C4 - genetics</subject><subject>Complement C4 - isolation & purification</subject><subject>Electrophoresis</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Humans</subject><subject>Isoelectric Focusing</subject><subject>Molecular Weight</subject><subject>Peptide Fragments - isolation & purification</subject><subject>Polymorphism, Genetic</subject><issn>0300-9475</issn><issn>1365-3083</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1981</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkU9O3DAUhy1URKfQIyBZXXTVhOfYTuIuKqHwX0ggtV1bcfLCeJTEUzsRzK5H6FW4CIfgJGQ0U7aIt_Hi-_3es_QR8oVBzKY5WsSMpzLikPOYqZzFgwGQaR4_7JDZK_pAZsABIiUy-ZF8CmEBwHiS8T2yl3EOKbAZuT9tsRq8W86dx8FW9Na1q8755dyGjrqGXoxd2dNCUBvoyYh0cLSYl_4O6YltGvTYVxio7ekwR_r0-Pz334Rt_43eegxT17Sr_7QQNT3z5V2H_XBAdpuyDfh5--6T32env4qL6Prm_LI4vo4qziSPmDR1hYlhjZENqFylKq9FiiprykRkiRGyTgXLOZSQJBIUU1waRGAMUiMzvk--bvYuvfszYhh0Z0OFbVv26MagM57nImHJm8HpN5lUgk3B75tg5V0IHhu99LYr_Uoz0Gs9eqHXDvTagV7r0Vs9-mEqH26vjKbD-rW69THxHxt-b1tcvWOz_nl1yYHzFzAkn7g</recordid><startdate>198109</startdate><enddate>198109</enddate><creator>MEVÅG, B.</creator><creator>OLAISEN, B.</creator><creator>TEISBERG, P.</creator><general>Blackwell Publishing Ltd</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>7T5</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>198109</creationdate><title>Electrophoretic Polymorphism of Human C4 is Due to Charge Differences in the α‐Chain, Presumably in the C4d Fragment</title><author>MEVÅG, B. ; OLAISEN, B. ; TEISBERG, P.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3153-15bdce2b1fb5f0989698d46e97fa2472b45d641830a0225091935bee01106b573</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1981</creationdate><topic>Complement C4 - genetics</topic><topic>Complement C4 - isolation & purification</topic><topic>Electrophoresis</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Humans</topic><topic>Isoelectric Focusing</topic><topic>Molecular Weight</topic><topic>Peptide Fragments - isolation & purification</topic><topic>Polymorphism, Genetic</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>MEVÅG, B.</creatorcontrib><creatorcontrib>OLAISEN, B.</creatorcontrib><creatorcontrib>TEISBERG, P.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Immunology Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Scandinavian journal of immunology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>MEVÅG, B.</au><au>OLAISEN, B.</au><au>TEISBERG, P.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Electrophoretic Polymorphism of Human C4 is Due to Charge Differences in the α‐Chain, Presumably in the C4d Fragment</atitle><jtitle>Scandinavian journal of immunology</jtitle><addtitle>Scand J Immunol</addtitle><date>1981-09</date><risdate>1981</risdate><volume>14</volume><issue>3</issue><spage>303</spage><epage>307</epage><pages>303-307</pages><issn>0300-9475</issn><eissn>1365-3083</eissn><abstract>Various common C4 gene products were isolated from serum by immunoprecipitation. After reduction the C4 α‐, β‐, and γ‐polypeptide chains were studied by two‐dimensional electrophoresis. Isoelectrofocusing was performed in the first dimension and sodium dodecyl sulphate polyacrylamide gradient gel electrophoresis in the second. The charge differences behind the electrophoretic C4 polymorphism were shown to reside in the 95,000‐u(atmic mass units) α‐chain. Charge variation closely mirroring the α‐chain differences were also found in a 49,000‐u fragment of the α‐chain, most probably C4d. The basic β‐chain could not be studied in detail, but no differences were observed with regard to molecular weight or charge of the γ‐chains of the different C4 gene products.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>7330601</pmid><doi>10.1111/j.1365-3083.1981.tb00568.x</doi><tpages>5</tpages></addata></record> |
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source | MEDLINE; Wiley Online Library Journals Frontfile Complete |
subjects | Complement C4 - genetics Complement C4 - isolation & purification Electrophoresis Electrophoresis, Polyacrylamide Gel Humans Isoelectric Focusing Molecular Weight Peptide Fragments - isolation & purification Polymorphism, Genetic |
title | Electrophoretic Polymorphism of Human C4 is Due to Charge Differences in the α‐Chain, Presumably in the C4d Fragment |
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