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The precursor of beta-lactamase: purification, properties and folding kinetics.
The precursor of Escherichia coli RTEM beta-lactamase was purified to homogeneity on a milligram scale by a procedure independent of the binding properties of the protein and refolded to an active, reduced form. For comparing the folding kinetics, the wild-type enzyme was reduced and a mutant was co...
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| Publicado no: | EMBO J |
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| Main Authors: | , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
Nature Publishing Group
1989
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC400976/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/2670555/ https://ncbi.nlm.nih.govhttps://doi.org/10.1002/j.1460-2075.1989.tb03530.x |
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