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The effect of organic cosolvents on the oxygen affinity of fetal hemoglobin: Relevance of protein-solvent interactions to the functional properties

✍ Scribed by Valeria Militello; Eugenio Vitrano; Antonio Cupane

Publisher
Elsevier Science
Year
1991
Tongue
English
Weight
782 KB
Volume
39
Category
Article
ISSN
0301-4622

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Effect of some organic cosolvents on the
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## Abstract We studied the effects of some organic cosolvents (monohydric alcohols and amides) on the reaction of hemoglobin with oxygen. We present evidence showing that our data can be analyzed within the framework of the Monod‐Wyman‐Changeux model and that the main effect of cosolvents is to alt

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We report on the effects that the presence of ethylene glycol or glycerol has on the oxygen affinity of hemoglobin. We attribute these effects to an altered equilibrium between T and R quaternary conformations of hernoglobin and separate them into hulk-electrostatic and non-bulk-electrostatic contri

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## Abstract We studied the effect of methanol, ethanol, __iso__‐propanol, and __n__‐propanol on the reaction of hemoglobin with oxygen. The oxygen affinity was found to decrease with increasing alcohol concentration and alkyl group size; no detectable effect on Hill's constant was found. Difference

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## Abstract We studied the kinetics of replacement of O~2~ by CO in hemoglobin in the presence and absence of organic cosolvents (methanol, ethanol, __iso__‐propanol, __n__‐propanol, formamide, acetamide, __N__‐methyl‐formamide) and at 10 and 25°C. Quantitative analysis of the results indicates tha