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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
13
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pubmed:dateCreated |
1984-8-20
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pubmed:abstractText |
The composition of the tubular structure of the membrane attack complex of complement (MAC) which migrates as a high molecular weight band (Mr approximately 1.2- 1.3 X 10(6) upon sodium dodecyl sulfate, polyacrylamide gel electrophoresis under reducing conditions was analyzed and compared to the high molecular weight band (Mr approximately 1.1 X 10(6] of tubular poly(C9). The sodium dodecyl sulfate-resistant band of the MAC, designated MAC-poly(C9), is composed of C6, C7, C8 alpha-gamma, and poly(C9), in approximate molar ratios of the protomers of 1:1:1:10-18. This conclusion is based 1) on the results of the incorporation of labeled proteins into MAC-poly(C9); 2) on the immunostaining of MAC-poly(C9) with anti-C6, anti-C7, anti-C8 alpha-gamma, and anti-C9 and its lack of immunostaining with anti-C5 and anti-C8 beta; and 3) on the dissociation of MAC-poly(C9) to 1 mol of C6, C7, C8 alpha-gamma and 10 to 18 mol of C9 upon treatment with 8 M guanidine isothiocyanate. Ultrastructurally the sodium dodecyl sulfate-resistant poly(C9) tubule and MAC-poly(C9) tubule are indistinguishable, suggesting a similar ultrastructure of the C6, C7, C8 alpha-gamma, and C9 subunits in the MAC-poly(C9) tubule. Further analogies among these four proteins are their tendency to form disulfide-linked dimers. It is concluded that the transmembrane channel of the MAC is formed by a tubule in which C6, C7, C8 alpha-gamma are copolymerized with poly(C9), whereas the C5b and C8 beta subunits are not part of the tubule structure and may form the 170-A long appendage of the MAC. This appendage is dissociated upon boiling in sodium dodecyl sulfate whereas the tubule remains stable.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Complement Membrane Attack Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Complement System Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Immune Sera,
http://linkedlifedata.com/resource/pubmed/chemical/Lipid Bilayers,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylcholines
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
259
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
8641-7
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:6736043-Complement Membrane Attack Complex,
pubmed-meshheading:6736043-Complement System Proteins,
pubmed-meshheading:6736043-Humans,
pubmed-meshheading:6736043-Immune Sera,
pubmed-meshheading:6736043-Lipid Bilayers,
pubmed-meshheading:6736043-Microscopy, Electron,
pubmed-meshheading:6736043-Molecular Weight,
pubmed-meshheading:6736043-Phosphatidylcholines,
pubmed-meshheading:6736043-Protein Conformation
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pubmed:year |
1984
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pubmed:articleTitle |
Molecular composition of the tubular structure of the membrane attack complex of complement.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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