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Study of the thermal denaturation of ribonuclease A by differential thermal analysis and susceptibility to proteolysis
1. The thermally induced change in conformation of ribonuclease A in solution was investigated by differential thermal analysis and the susceptibility of the enzyme to proteolytic digestion by ficin. 2. A transition with a mid-point of 60.5°C at pH4.2 was observed directly by differential thermal an...
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| Autori principali: | , , |
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| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
1970
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1178862/ https://ncbi.nlm.nih.gov/pubmed/5463263 |
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