Complement Lysis: the Ultrastructure and Orientation of the C5b-9 Complex on Target Sheep Erythrocyte Membranes
The C5b-9 complex derived from human serum and assembled on target sheep erythrocyte membranes is a thin-walled cylinder rimmed by an annulus at one end. The total height of the cylinder is 150 Å, towards which the annulus contributes 30 Å. The cylinder has an apparently uniform internal diameter of...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
TRANUM-JENSEN, J. [verfasserIn] BHAKDI, S. [verfasserIn] BHAKDI-LEHNEN, B. [verfasserIn] |
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| Format: |
E-Artikel |
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| Erschienen: |
Oxford, UK: Blackwell Publishing Ltd ; 1978 |
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| Umfang: |
Online-Ressource |
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| Reproduktion: |
2006 ; Blackwell Publishing Journal Backfiles 1879-2005 |
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| Übergeordnetes Werk: |
In: Scandinavian journal of immunology - Oxford [u.a.] : Wiley-Blackwell, 1972, 7(1978), 1, Seite 0 |
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volume:7 ; year:1978 ; number:1 ; pages:0 |
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| DOI / URN: |
10.1111/j.1365-3083.1978.tb00425.x |
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| 520 | |a The C5b-9 complex derived from human serum and assembled on target sheep erythrocyte membranes is a thin-walled cylinder rimmed by an annulus at one end. The total height of the cylinder is 150 Å, towards which the annulus contributes 30 Å. The cylinder has an apparently uniform internal diameter of 100 Å. The external diameter of the annulus is 200 Å. The classical complement ‘rings’ visualized on membranes after complement lysis represent such C5b-9 cylinders perpendicularly oriented on the membranes. The thin-walled cylinder is anchored in the membrane maim and the annulus located in the exterior membrane glycocalyx. At the sites of attachment of the C5b-9 complexes, the continuity of the membrane bilayer is disturbed and the presence of trans-membrane pores is indicated The data essentially support the ‘doughnut’ theory of complement lysis. | ||
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10.1111/j.1365-3083.1978.tb00425.x doi (DE-627)NLEJ241938023 DE-627 ger DE-627 rakwb TRANUM-JENSEN, J. verfasserin aut Complement Lysis: the Ultrastructure and Orientation of the C5b-9 Complex on Target Sheep Erythrocyte Membranes Oxford, UK Blackwell Publishing Ltd 1978 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The C5b-9 complex derived from human serum and assembled on target sheep erythrocyte membranes is a thin-walled cylinder rimmed by an annulus at one end. The total height of the cylinder is 150 Å, towards which the annulus contributes 30 Å. The cylinder has an apparently uniform internal diameter of 100 Å. The external diameter of the annulus is 200 Å. The classical complement ‘rings’ visualized on membranes after complement lysis represent such C5b-9 cylinders perpendicularly oriented on the membranes. The thin-walled cylinder is anchored in the membrane maim and the annulus located in the exterior membrane glycocalyx. At the sites of attachment of the C5b-9 complexes, the continuity of the membrane bilayer is disturbed and the presence of trans-membrane pores is indicated The data essentially support the ‘doughnut’ theory of complement lysis. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| BHAKDI, S. verfasserin aut BHAKDI-LEHNEN, B. verfasserin aut BJERRUM, O. J. oth SPETH, V. oth In Scandinavian journal of immunology Oxford [u.a.] : Wiley-Blackwell, 1972 7(1978), 1, Seite 0 Online-Ressource (DE-627)NLEJ24392724X (DE-600)2020954-X 1365-3083 nnns volume:7 year:1978 number:1 pages:0 http://dx.doi.org/10.1111/j.1365-3083.1978.tb00425.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 7 1978 1 0 |
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10.1111/j.1365-3083.1978.tb00425.x doi (DE-627)NLEJ241938023 DE-627 ger DE-627 rakwb TRANUM-JENSEN, J. verfasserin aut Complement Lysis: the Ultrastructure and Orientation of the C5b-9 Complex on Target Sheep Erythrocyte Membranes Oxford, UK Blackwell Publishing Ltd 1978 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The C5b-9 complex derived from human serum and assembled on target sheep erythrocyte membranes is a thin-walled cylinder rimmed by an annulus at one end. The total height of the cylinder is 150 Å, towards which the annulus contributes 30 Å. The cylinder has an apparently uniform internal diameter of 100 Å. The external diameter of the annulus is 200 Å. The classical complement ‘rings’ visualized on membranes after complement lysis represent such C5b-9 cylinders perpendicularly oriented on the membranes. The thin-walled cylinder is anchored in the membrane maim and the annulus located in the exterior membrane glycocalyx. At the sites of attachment of the C5b-9 complexes, the continuity of the membrane bilayer is disturbed and the presence of trans-membrane pores is indicated The data essentially support the ‘doughnut’ theory of complement lysis. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| BHAKDI, S. verfasserin aut BHAKDI-LEHNEN, B. verfasserin aut BJERRUM, O. J. oth SPETH, V. oth In Scandinavian journal of immunology Oxford [u.a.] : Wiley-Blackwell, 1972 7(1978), 1, Seite 0 Online-Ressource (DE-627)NLEJ24392724X (DE-600)2020954-X 1365-3083 nnns volume:7 year:1978 number:1 pages:0 http://dx.doi.org/10.1111/j.1365-3083.1978.tb00425.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 7 1978 1 0 |
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10.1111/j.1365-3083.1978.tb00425.x doi (DE-627)NLEJ241938023 DE-627 ger DE-627 rakwb TRANUM-JENSEN, J. verfasserin aut Complement Lysis: the Ultrastructure and Orientation of the C5b-9 Complex on Target Sheep Erythrocyte Membranes Oxford, UK Blackwell Publishing Ltd 1978 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The C5b-9 complex derived from human serum and assembled on target sheep erythrocyte membranes is a thin-walled cylinder rimmed by an annulus at one end. The total height of the cylinder is 150 Å, towards which the annulus contributes 30 Å. The cylinder has an apparently uniform internal diameter of 100 Å. The external diameter of the annulus is 200 Å. The classical complement ‘rings’ visualized on membranes after complement lysis represent such C5b-9 cylinders perpendicularly oriented on the membranes. The thin-walled cylinder is anchored in the membrane maim and the annulus located in the exterior membrane glycocalyx. At the sites of attachment of the C5b-9 complexes, the continuity of the membrane bilayer is disturbed and the presence of trans-membrane pores is indicated The data essentially support the ‘doughnut’ theory of complement lysis. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| BHAKDI, S. verfasserin aut BHAKDI-LEHNEN, B. verfasserin aut BJERRUM, O. J. oth SPETH, V. oth In Scandinavian journal of immunology Oxford [u.a.] : Wiley-Blackwell, 1972 7(1978), 1, Seite 0 Online-Ressource (DE-627)NLEJ24392724X (DE-600)2020954-X 1365-3083 nnns volume:7 year:1978 number:1 pages:0 http://dx.doi.org/10.1111/j.1365-3083.1978.tb00425.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 7 1978 1 0 |
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10.1111/j.1365-3083.1978.tb00425.x doi (DE-627)NLEJ241938023 DE-627 ger DE-627 rakwb TRANUM-JENSEN, J. verfasserin aut Complement Lysis: the Ultrastructure and Orientation of the C5b-9 Complex on Target Sheep Erythrocyte Membranes Oxford, UK Blackwell Publishing Ltd 1978 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The C5b-9 complex derived from human serum and assembled on target sheep erythrocyte membranes is a thin-walled cylinder rimmed by an annulus at one end. The total height of the cylinder is 150 Å, towards which the annulus contributes 30 Å. The cylinder has an apparently uniform internal diameter of 100 Å. The external diameter of the annulus is 200 Å. The classical complement ‘rings’ visualized on membranes after complement lysis represent such C5b-9 cylinders perpendicularly oriented on the membranes. The thin-walled cylinder is anchored in the membrane maim and the annulus located in the exterior membrane glycocalyx. At the sites of attachment of the C5b-9 complexes, the continuity of the membrane bilayer is disturbed and the presence of trans-membrane pores is indicated The data essentially support the ‘doughnut’ theory of complement lysis. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| BHAKDI, S. verfasserin aut BHAKDI-LEHNEN, B. verfasserin aut BJERRUM, O. J. oth SPETH, V. oth In Scandinavian journal of immunology Oxford [u.a.] : Wiley-Blackwell, 1972 7(1978), 1, Seite 0 Online-Ressource (DE-627)NLEJ24392724X (DE-600)2020954-X 1365-3083 nnns volume:7 year:1978 number:1 pages:0 http://dx.doi.org/10.1111/j.1365-3083.1978.tb00425.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 7 1978 1 0 |
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10.1111/j.1365-3083.1978.tb00425.x doi (DE-627)NLEJ241938023 DE-627 ger DE-627 rakwb TRANUM-JENSEN, J. verfasserin aut Complement Lysis: the Ultrastructure and Orientation of the C5b-9 Complex on Target Sheep Erythrocyte Membranes Oxford, UK Blackwell Publishing Ltd 1978 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The C5b-9 complex derived from human serum and assembled on target sheep erythrocyte membranes is a thin-walled cylinder rimmed by an annulus at one end. The total height of the cylinder is 150 Å, towards which the annulus contributes 30 Å. The cylinder has an apparently uniform internal diameter of 100 Å. The external diameter of the annulus is 200 Å. The classical complement ‘rings’ visualized on membranes after complement lysis represent such C5b-9 cylinders perpendicularly oriented on the membranes. The thin-walled cylinder is anchored in the membrane maim and the annulus located in the exterior membrane glycocalyx. At the sites of attachment of the C5b-9 complexes, the continuity of the membrane bilayer is disturbed and the presence of trans-membrane pores is indicated The data essentially support the ‘doughnut’ theory of complement lysis. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| BHAKDI, S. verfasserin aut BHAKDI-LEHNEN, B. verfasserin aut BJERRUM, O. J. oth SPETH, V. oth In Scandinavian journal of immunology Oxford [u.a.] : Wiley-Blackwell, 1972 7(1978), 1, Seite 0 Online-Ressource (DE-627)NLEJ24392724X (DE-600)2020954-X 1365-3083 nnns volume:7 year:1978 number:1 pages:0 http://dx.doi.org/10.1111/j.1365-3083.1978.tb00425.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 7 1978 1 0 |
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The C5b-9 complex derived from human serum and assembled on target sheep erythrocyte membranes is a thin-walled cylinder rimmed by an annulus at one end. The total height of the cylinder is 150 Å, towards which the annulus contributes 30 Å. The cylinder has an apparently uniform internal diameter of 100 Å. The external diameter of the annulus is 200 Å. The classical complement ‘rings’ visualized on membranes after complement lysis represent such C5b-9 cylinders perpendicularly oriented on the membranes. The thin-walled cylinder is anchored in the membrane maim and the annulus located in the exterior membrane glycocalyx. At the sites of attachment of the C5b-9 complexes, the continuity of the membrane bilayer is disturbed and the presence of trans-membrane pores is indicated The data essentially support the ‘doughnut’ theory of complement lysis. |
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The C5b-9 complex derived from human serum and assembled on target sheep erythrocyte membranes is a thin-walled cylinder rimmed by an annulus at one end. The total height of the cylinder is 150 Å, towards which the annulus contributes 30 Å. The cylinder has an apparently uniform internal diameter of 100 Å. The external diameter of the annulus is 200 Å. The classical complement ‘rings’ visualized on membranes after complement lysis represent such C5b-9 cylinders perpendicularly oriented on the membranes. The thin-walled cylinder is anchored in the membrane maim and the annulus located in the exterior membrane glycocalyx. At the sites of attachment of the C5b-9 complexes, the continuity of the membrane bilayer is disturbed and the presence of trans-membrane pores is indicated The data essentially support the ‘doughnut’ theory of complement lysis. |
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The C5b-9 complex derived from human serum and assembled on target sheep erythrocyte membranes is a thin-walled cylinder rimmed by an annulus at one end. The total height of the cylinder is 150 Å, towards which the annulus contributes 30 Å. The cylinder has an apparently uniform internal diameter of 100 Å. The external diameter of the annulus is 200 Å. The classical complement ‘rings’ visualized on membranes after complement lysis represent such C5b-9 cylinders perpendicularly oriented on the membranes. The thin-walled cylinder is anchored in the membrane maim and the annulus located in the exterior membrane glycocalyx. At the sites of attachment of the C5b-9 complexes, the continuity of the membrane bilayer is disturbed and the presence of trans-membrane pores is indicated The data essentially support the ‘doughnut’ theory of complement lysis. |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ241938023</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707144011.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">120427s1978 xx |||||o 00| ||und c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1111/j.1365-3083.1978.tb00425.x</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ241938023</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">TRANUM-JENSEN, J.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Complement Lysis: the Ultrastructure and Orientation of the C5b-9 Complex on Target Sheep Erythrocyte Membranes</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="a">Oxford, UK</subfield><subfield code="b">Blackwell Publishing Ltd</subfield><subfield code="c">1978</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">The C5b-9 complex derived from human serum and assembled on target sheep erythrocyte membranes is a thin-walled cylinder rimmed by an annulus at one end. The total height of the cylinder is 150 Å, towards which the annulus contributes 30 Å. The cylinder has an apparently uniform internal diameter of 100 Å. The external diameter of the annulus is 200 Å. The classical complement ‘rings’ visualized on membranes after complement lysis represent such C5b-9 cylinders perpendicularly oriented on the membranes. The thin-walled cylinder is anchored in the membrane maim and the annulus located in the exterior membrane glycocalyx. At the sites of attachment of the C5b-9 complexes, the continuity of the membrane bilayer is disturbed and the presence of trans-membrane pores is indicated The data essentially support the ‘doughnut’ theory of complement lysis.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="d">2006</subfield><subfield code="f">Blackwell Publishing Journal Backfiles 1879-2005</subfield><subfield code="7">|2006||||||||||</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">BHAKDI, S.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">BHAKDI-LEHNEN, B.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">BJERRUM, O. 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7.39993 |