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Allosteric kinetics and equilibria differ for carbon monoxide and oxygen binding to hemoglobin.
We have measured the forward and reverse rates of the allosteric transition between R (relaxed) and T (tense) quaternary structures for oxyhemoglobin A from which a single oxygen molecule was removed in pH 7, phosphate buffer, using the method of modulated excitation (Ferrone, F.A., and J.J. Hopfiel...
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| Main Authors: | , , |
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| Format: | Artigo |
| Sprog: | Inglês |
| Udgivet: |
The Biophysical Society
1990
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| Fag: | |
| Online adgang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1280975/ https://ncbi.nlm.nih.gov/pubmed/2207241 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/S0006-3495(90)82380-8 |
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