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Oxygen affinity of bovine haemoglobin: Relevance of electrostatic and hydrophobic interactions

✍ Scribed by Eugenio Vitrano; Antonio Cupane; Lorenzo Cordone

Book ID
118918537
Publisher
Elsevier Science
Year
1984
Tongue
English
Weight
923 KB
Volume
180
Category
Article
ISSN
0022-2836

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## Abstract We studied the kinetics of the heat denaturation (at 50Β°C) of met‐hemoglobin 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