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The refolding of hen egg white riboflavin-binding protein: effect of protein disulphide isomerase on the reoxidation of the reduced protein.
Hen egg white riboflavin-binding protein (RfBP) contains nine disulphide bonds. Provided these remain intact, the refolding of RfBP after incubation in 6 M guanidinium chloride is highly efficient with at least 95% of the binding activity regained within 3 min. Kinetic studies indicate that this reg...
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| Autori principali: | , , , |
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| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
1995
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1136129/ https://ncbi.nlm.nih.gov/pubmed/7575444 |
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