Stabilization of apoglobin by low temperature increases yield of soluble recombinant hemoglobin in Escherichia coli.
Accumulation of soluble recombinant hemoglobin (rHb1.1) in Escherichia coli requires proper protein folding, prosthetic group (heme) addition, and subunit assembly. This served as a new model system for the study of the effects of temperature, protein synthesis rates, and protein accumulation rates...
Uloženo v:
| Vydáno v: | Appl Environ Microbiol |
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| Hlavní autoři: | , , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
American Society for Microbiology (ASM)
1997
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC168751/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/9361418/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/aem.63.11.4313-4320.1997 |
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