## Abstract The binding of azide ion to horse‐heart myoglobins has been studied at pH 6.98 and at various temperatures. The results show that the azide complex is not completely loe spin and that the spin population is strongly dependent on temperature. We have shown that with some assumption it is
Binding of azide ion to methemoglobin at elevated temperatures and the reality of the “compensation” temperature
✍ Scribed by A. C. I. Anusiem; G. B. Ogunmola; J. G. Beetlestone
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1977
- Tongue
- English
- Weight
- 268 KB
- Volume
- 16
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Abstract
We have studied the binding of azide ion to ferrihemoglobin at elevated temperatures. Up to a temperature of 45°C there is no difference in the ligand binding behavior of hemoglobin when compared with the results obtained at lower temperatures. The compensation temperature Tc of 290.6 ± 5.3°K, obtained in this study within the temperature range 303–318°K, confirms that the compensation pattern obtained by Lumry and Rajender is not dependent on the temperature range of the experiment but an intrinsic property of the protein conformation.
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concentration of this certain component and relatively m a l l weights are used for the other components. Furthermore, instead of the least squares criterion, any other criterion can also be used in the procedure discussed above. ## An estimation problem with multipoint boundary value (3) in diff