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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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Autors principals: Ramm, L E, Whitlow, M B, Mayer, M M
Format: Artigo
Idioma:Inglês
Publicat: 1982
Matèries:
Accés en línia:https://ncbi.nlm.nih.gov/pmc/articles/PMC346755/
https://ncbi.nlm.nih.gov/pubmed/6289316
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