Allosteric effectors do not alter the oxygen affinity of hemoglobin crystals.
Mozzarelli A, Rivetti C, Rossi GL, Eaton WA, Henry ER.
Mozzarelli A, et al. Among authors: rivetti c.
Protein Sci. 1997 Feb;6(2):484-9. doi: 10.1002/pro.5560060230.
Protein Sci. 1997.
PMID: 9041656
Free PMC article.
To explain these effects, as well as the absence of the Bohr effect and the lower oxygen affinity of T-state hemoglobin in the crystal compared to solution, Rivetti C et al. (1993a, Biochemistry 32:2888-2906) suggested that there are high- and low-affinity subunit c …
To explain these effects, as well as the absence of the Bohr effect and the lower oxygen affinity of T-state hemoglobin in the crystal compa …