Studies on carbon monoxide binding by shark haemoglobin.
The kinetics of the reactions of Pacific-porbeagle haemoglobin with CO were studied by flash-photolysis and stopped-flow methods, and the equilibrium binding curves for CO were measured in spectrophotometric titrations. Measurements were made in the pH range 6-8 and in the temperature range 0-40 deg...
| Main Authors: | , |
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| Format: | Text |
| Language: | English |
| Published: |
1981
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| Subjects: | |
| Online Access: | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1163144 http://www.ncbi.nlm.nih.gov/pubmed/7325965 |
| Summary: | The kinetics of the reactions of Pacific-porbeagle haemoglobin with CO were studied by flash-photolysis and stopped-flow methods, and the equilibrium binding curves for CO were measured in spectrophotometric titrations. Measurements were made in the pH range 6-8 and in the temperature range 0-40 degrees C. The results are discussed in terms of the allosteric model proposed by Monod, Wyman & Changeux [(1965) J. Mol. Biol. 12, 88-118]. Within this framework the results indicate that in the R-state the haem groups fall into two classes of different reactivity with different spectral characteristics, but that in the T-state the groups may be essentially equivalent. The physiological importance of the temperature-insensitivity of the equilibrium ligand-binding curves for porbeagle haemoglobin is discussed. |
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