Both the Fast and Slow Refolding Reactions of Ribonuclease A Yield Native Enzyme
The fast reaction ((T̄2) ≃ 50 msec) observed previously in the refolding of thermally unfolded ribonuclease A (disulfide bonds intact) has now been studied by two properties indicative of enzyme function: binding of a competitive inhibitor (2′CMP) and hydrolysis of a substrate (CpA → C > p + A). Bot...
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| Vydáno v: | Proc Natl Acad Sci U S A |
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| Hlavní autoři: | , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
National Academy of Sciences
1973
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC427234/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/4519627/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.70.12.3347 |
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