Ultrastructure of the First Component of Human Complement: Electron Microscopy of the Crosslinked Complex
Electron micrographs are shown of the first component of human complement (C1) which has been crosslinked with a water-soluble carbodiimide to prevent dissociation into its C1q and C1r2C1s2subunits. Two projections of the crosslinked molecule are seen in the electron micrographs, which are called ``...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1982-01, Vol.79 (2), p.586-590 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Strang, Candace J. Siegel, Richard C. Phillips, Martin L. Poon, Pak H. Schumaker, Verne N. |
| description | Electron micrographs are shown of the first component of human complement (C1) which has been crosslinked with a water-soluble carbodiimide to prevent dissociation into its C1q and C1r2C1s2subunits. Two projections of the crosslinked molecule are seen in the electron micrographs, which are called ``top'' and ``profile.'' In both views, the C1q heads are visible. From the top, the C1r2C1s2tetrameric subunit appears to be located centrally on the C1q and folded to form a compact mass obscuring most of the arms and central bundle. In profile, the tetramer appears to be located in the region of the arms between the C1q heads and the central bundle. Both the heads and the rod-like central bundle appear to be free of C1r2C1s2in these profile projections. Sometimes it is possible to count more than six domains in the region of the C1q heads, as though a portion of the tetramer had unfolded to protrude among the heads. |
| doi_str_mv | 10.1073/pnas.79.2.586 |
| format | Article |
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Two projections of the crosslinked molecule are seen in the electron micrographs, which are called ``top'' and ``profile.'' In both views, the C1q heads are visible. From the top, the C1r2C1s2tetrameric subunit appears to be located centrally on the C1q and folded to form a compact mass obscuring most of the arms and central bundle. In profile, the tetramer appears to be located in the region of the arms between the C1q heads and the central bundle. Both the heads and the rod-like central bundle appear to be free of C1r2C1s2in these profile projections. 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Two projections of the crosslinked molecule are seen in the electron micrographs, which are called ``top'' and ``profile.'' In both views, the C1q heads are visible. From the top, the C1r2C1s2tetrameric subunit appears to be located centrally on the C1q and folded to form a compact mass obscuring most of the arms and central bundle. In profile, the tetramer appears to be located in the region of the arms between the C1q heads and the central bundle. Both the heads and the rod-like central bundle appear to be free of C1r2C1s2in these profile projections. Sometimes it is possible to count more than six domains in the region of the C1q heads, as though a portion of the tetramer had unfolded to protrude among the heads.</description><subject>Antibodies</subject><subject>Biochemistry</subject><subject>Carbodiimides</subject><subject>Complement C1</subject><subject>Cross-Linking Reagents</subject><subject>Crosslinking</subject><subject>Electron micrographs</subject><subject>Electron microscopy</subject><subject>Gels</subject><subject>Humans</subject><subject>Immunology</subject><subject>Macromolecular Substances</subject><subject>man</subject><subject>Microscopy, Electron</subject><subject>Molecules</subject><subject>Protein Conformation</subject><subject>Quaternary ammonium compounds</subject><subject>ultrastructure</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1982</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkcFP5CAUxolxo6Pr0YvRpBe9dRYoLcXEg5nouonGi54JpaBVWipQM_73Uqfj6mU3ISG87_e9vMcHwD6CcwRp9qvvhJ9TNsfzvCw2wAxBhtKCMLgJZhBimpYEk22w4_0ThJDlJdwCWwXLMUZwBpp7E5zwwQ0yDE4lVifhUSWXjfMhWdi2t53qwli-GlrRfZSMamPtNLkwSgZnu-Smkc56afu3tX8R39403bOqJ8vyJ_ihhfFqb7p3wf3lxd3iKr2-_f1ncX6dSlLikFJasrIgmSyrXCsRTyVwTpEWSOIqiwuQAiJR67rGVGqmtK6KutKCVqKGucx2wdmqbz9UraplHNUJw3vXtMK9cSsa_l3pmkf-YF95RnLKYPSfTH5nXwblA28bL5UxolN28JwSSMsCk_-CKCcMEZJFMF2B4y95p_TnMAjyMUM-Zsgp45jHDCN_9HWDT3oKLerHkz7a1urazvVgTFDLELnDf3BRPljJTz5Y93cmjHCWvQMKkrxH</recordid><startdate>19820101</startdate><enddate>19820101</enddate><creator>Strang, Candace J.</creator><creator>Siegel, Richard C.</creator><creator>Phillips, Martin L.</creator><creator>Poon, Pak H.</creator><creator>Schumaker, Verne N.</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</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>7QL</scope><scope>7T5</scope><scope>C1K</scope><scope>H94</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19820101</creationdate><title>Ultrastructure of the First Component of Human Complement: Electron Microscopy of the Crosslinked Complex</title><author>Strang, Candace J. ; Siegel, Richard C. ; Phillips, Martin L. ; Poon, Pak H. ; Schumaker, Verne N.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c482t-77898643c8b5feafeaba2571fa1c2b30954601adfdd27cf9effb6dbfa7bad05c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1982</creationdate><topic>Antibodies</topic><topic>Biochemistry</topic><topic>Carbodiimides</topic><topic>Complement C1</topic><topic>Cross-Linking Reagents</topic><topic>Crosslinking</topic><topic>Electron micrographs</topic><topic>Electron microscopy</topic><topic>Gels</topic><topic>Humans</topic><topic>Immunology</topic><topic>Macromolecular Substances</topic><topic>man</topic><topic>Microscopy, Electron</topic><topic>Molecules</topic><topic>Protein Conformation</topic><topic>Quaternary ammonium compounds</topic><topic>ultrastructure</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Strang, Candace J.</creatorcontrib><creatorcontrib>Siegel, Richard C.</creatorcontrib><creatorcontrib>Phillips, Martin L.</creatorcontrib><creatorcontrib>Poon, Pak H.</creatorcontrib><creatorcontrib>Schumaker, Verne N.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Immunology Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Strang, Candace J.</au><au>Siegel, Richard C.</au><au>Phillips, Martin L.</au><au>Poon, Pak H.</au><au>Schumaker, Verne N.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Ultrastructure of the First Component of Human Complement: Electron Microscopy of the Crosslinked Complex</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1982-01-01</date><risdate>1982</risdate><volume>79</volume><issue>2</issue><spage>586</spage><epage>590</epage><pages>586-590</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Electron micrographs are shown of the first component of human complement (C1) which has been crosslinked with a water-soluble carbodiimide to prevent dissociation into its C1q and C1r2C1s2subunits. Two projections of the crosslinked molecule are seen in the electron micrographs, which are called ``top'' and ``profile.'' In both views, the C1q heads are visible. From the top, the C1r2C1s2tetrameric subunit appears to be located centrally on the C1q and folded to form a compact mass obscuring most of the arms and central bundle. In profile, the tetramer appears to be located in the region of the arms between the C1q heads and the central bundle. Both the heads and the rod-like central bundle appear to be free of C1r2C1s2in these profile projections. Sometimes it is possible to count more than six domains in the region of the C1q heads, as though a portion of the tetramer had unfolded to protrude among the heads.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>6952210</pmid><doi>10.1073/pnas.79.2.586</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1982-01, Vol.79 (2), p.586-590 |
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| source | Jstor Complete Legacy; MEDLINE; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Antibodies Biochemistry Carbodiimides Complement C1 Cross-Linking Reagents Crosslinking Electron micrographs Electron microscopy Gels Humans Immunology Macromolecular Substances man Microscopy, Electron Molecules Protein Conformation Quaternary ammonium compounds ultrastructure |
| title | Ultrastructure of the First Component of Human Complement: Electron Microscopy of the Crosslinked Complex |
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