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Heat-induced denaturation and aggregation of ovalbumin at neutral pH described by irreversible first-order kinetics
The heat-induced denaturation kinetics of two different sources of ovalbumin at pH 7 was studied by chromatography and differential scanning calorimetry. The kinetics was found to be independent of protein concentration and salt concentration, but was strongly dependent on temperature. For highly pu...
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| Hauptverfasser: | , , , |
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| Format: | Artigo |
| Sprache: | Inglês |
| Veröffentlicht: |
Cold Spring Harbor Laboratory Press
2003
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| Schlagworte: | |
| Online Zugang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2366979/ https://ncbi.nlm.nih.gov/pubmed/14627731 |
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