Chemical and immunological analysis of the complex structure of Escherichia coli alpha-hemolysin.
Escherichia coli alpha-hemolysin (AH) purified from culture supernatants by gel filtration and ion-exchange chromatography was heterogeneous in charge and size. A 107,000-dalton protein was identified as the product of the hlyA gene by its reactivity with anti-AH monoclonal antibodies. Proteolysis o...
Uloženo v:
| Vydáno v: | J Bacteriol |
|---|---|
| Hlavní autoři: | , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
American Society for Microbiology (ASM)
1985
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC219299/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/3905764/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.164.3.1071-1080.1985 |
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