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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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Sonraí Bibleagrafaíochta
Main Authors: Zhang, N. Q., Ferrone, F. A., Martino, A. J.
Formáid: Artigo
Teanga:Inglês
Foilsithe: The Biophysical Society 1990
Ábhair:
Rochtain Ar Líne: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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