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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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Bibliografische Detailangaben
Veröffentlicht in:Proc Natl Acad Sci U S A
Hauptverfasser: Garel, Jean-Renaud, Baldwin, Robert L.
Format: Artigo
Sprache:Inglês
Veröffentlicht: National Academy of Sciences 1973
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Online-Zugang: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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