Marit Nilsen‐Hamilton, Stuart J. Edelstein
Abstract
Cat hemoglobin has a lower cooperativity and oxygen affinity than most mammalian hemoglobins. In contrast to the usual invariance of cooperativity with pH, a rise in cooperativity with pH is predicted by the allosteric model for low-affinity hemoglobins. Such a pH-dependent cooperativity for cat hemoglobin has been found.
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Cat hemoglobin has a lower cooperativity and oxygen affinity than most mammalian hemoglobins. In contrast to the usual invariance of cooperativity with pH, a rise in cooperativity with pH is predicted by the allosteric model for low-affinity hemoglobins. Such a pH-dependent cooperativity for cat hemoglobin has been found.
Key concepts: Cooperativity, Allosteric regulation, Hemoglobin, Chemistry, Cooperative binding, Biophysics, Oxygen, Biochemistry