Apparent molecular weights of a heat-modifiable protein from the outer membrane of Escherichia coli in gels with different acrylamide concentrations.
The apparent molecular weights of the two forms of a heat-modifiable protein from the outer membrane of Escherichia coli K-12, estimated in gels with different concentrations of acrylamide, indicate that the protein binds excess amounts of sodium dodecyl sulfate, possibly due to large beta structure...
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| Опубликовано в:: | J Bacteriol |
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| Главный автор: | |
| Формат: | Artigo |
| Язык: | Inglês |
| Опубликовано: |
American Society for Microbiology (ASM)
1978
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| Предметы: | |
| Online-ссылка: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC222370/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/350841/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.134.3.1181-1183.1978 |
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