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The cytolytic toxin aerolysin must aggregate to disrupt erythrocytes, and aggregation is stimulated by human glycophorin.
The hole-forming toxin aerolysin was shown to aggregate after binding to erythrocytes at 37 degrees C. Although the protein also bound and aggregated at 4 degrees C, hole formation was not observed, indicating that aggregation preceded penetration of the lipid bilayer. Aggregation, but not binding,...
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| Auteurs principaux: | , |
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| Format: | Artigo |
| Langue: | Inglês |
| Publié: |
1988
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| Sujets: | |
| Accès en ligne: | https://ncbi.nlm.nih.gov/pmc/articles/PMC259800/ https://ncbi.nlm.nih.gov/pubmed/3281905 |
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