Purification of cereolysin and the electrophoretic separation of the active (reduced) and inactive (oxidized) forms of the purified toxin.
Cereolysin was purified to apparent homogeneity by using ammonium sulfate fractionation, hydrophobic chromatography with AH-Sepharose, isoelectric focusing, and gel filtration. The active form of the toxin had an isoelectric point of 6.6, and the molecular weight of the protein was about 55,500 as j...
Gardado en:
| Publicado en: | Infect Immun |
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| Principais autores: | , , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado: |
American Society for Microbiology (ASM)
1976
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| Assuntos: | |
| Acceso en liña: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC420857/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/820638/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/iai.14.1.144-154.1976 |
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