## Abstract We studied the kinetics of the heat denaturation (at 50Β°C) of metβhemoglobin in the presence of various monohydric alcohols. The denaturation rate was slowed by the presence of small concentrations of methanol and ethanol; in all the other cases, i.e., at high concentrations of methanol
Conformational and functional properties of haemoglobin in perturbed solvent: Relevance of electrostatic and hydrophobic interactions.
β Scribed by Lorenzo Cordone; Antonio Cupane; Eugenio Vitrano
- Book ID
- 103594082
- Publisher
- Elsevier Science
- Year
- 1989
- Tongue
- English
- Weight
- 981 KB
- Volume
- 42
- Category
- Article
- ISSN
- 0167-7322
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