Transmembrane channel formation by complement: functional analysis of the number of C5b6, C7, C8, and C9 molecules required for a single channel.
Earlier studies have shown that sequential treatment of resealed erythrocyte ghosts with C5b6, C7, C8, and C9 leads to insertion of hydrophobic peptides from these complement proteins into the membrane and assembly of transmembrane channels. The number of molecules of each of the proteins required f...
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| Pubblicato in: | Proc Natl Acad Sci U S A |
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| Autori principali: | , , |
| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
National Academy of Sciences
1982
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC346755/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/6289316/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.79.15.4751 |
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