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
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
No coin nor oath required. For personal study only.
✦ 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