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High and low oxygen affinity conformations of T state hemoglobin.
Bruno S, Bonaccio M, Bettati S, Rivetti C, Viappiani C, Abbruzzetti S, Mozzarelli A. Bruno S, et al. Among authors: rivetti c. Protein Sci. 2001 Nov;10(11):2401-7. doi: 10.1110/ps.20501. Protein Sci. 2001. PMID: 11604545 Free PMC article.
Oxygen binding by single crystals of hemoglobin.
Rivetti C, Mozzarelli A, Rossi GL, Henry ER, Eaton WA. Rivetti C, et al. Biochemistry. 1993 Mar 23;32(11):2888-906. doi: 10.1021/bi00062a021. Biochemistry. 1993. PMID: 8457555
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 …
83 results