Abstract
Dichloromethane is an anesthetic that weakdy binds to hemoglobin at four different sites. It also reduces the gelation of hemoglobin S. Hemoglobin oxygenation curves have been measured for different partial pressures of dichloromethane. These curves show that the binding of oxygen to hemoglobin remains cooperative in the presence of dichloromethane. Application of the thermodynamic approach suggests that only one of the binding sites is responsible for decreasing the oxygen-affinity of hemoglobin.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Enzymology
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