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The Cu,Zn superoxide dismutase from Escherichia coli retains monomeric structure at high protein concentration. Evidence for altered subunit interaction in all the bacteriocupreins.
Gel-filtration chromatography experiments performed at high protein concentrations demonstrate that the Cu,Zn superoxide dismutase from Escherichia coli is monomeric irrespective of the buffer and of ionic strength. The catalytic activity of the recombinant enzyme is comparable with that of eukaryot...
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| Autores principales: | , , , , |
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| Formato: | Artigo |
| Lenguaje: | Inglês |
| Publicado: |
1996
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| Materias: | |
| Acceso en línea: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1217988/ https://ncbi.nlm.nih.gov/pubmed/9003353 |
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