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Effects of some organic cosolvents on the functional properties of hemoglobin: Kinetics of O2 displacement by CO

✍ Scribed by Lorenzo Cordone; Antonio Cupane


Publisher
Wiley (John Wiley & Sons)
Year
1981
Tongue
English
Weight
311 KB
Volume
20
Category
Article
ISSN
0006-3525

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✦ Synopsis


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 that these cosolvents do not affect the intrinsic binding constants of ligands to the heme when hemoglobin is in the R conformation. The present results confirm the previously reported suggestion that the effects of the above cosolvents on the oxygen affinity of hemoglobin are related to effects on the T ⇄ R conformational equilibrium.


📜 SIMILAR VOLUMES


Conformational and functional properties
✍ Donatella Bulone; Antonio Cupane; Lorenzo Cordone 📂 Article 📅 1983 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 215 KB

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