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THE REVERSIBLE HEAT DENATURATION OF CHYMOTRYPSINOGEN
Within a restricted range of pH and protein concentration crystalline chymotrypsinogen undergoes thermal denaturation which is wholly reversed upon cooling. At a given temperature an equilibrium exists between native and reversibly denatured protein. Within the pH range 2 to 3 the amount of denature...
| Autores principales: | , |
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| Formato: | Texto |
| Lenguaje: | English |
| Publicado: |
The Rockefeller University Press
1951
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| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2147273/ https://www.ncbi.nlm.nih.gov/pubmed/14832440 |