PREVIOUS results have shown that two of the haemoglobin components from trout blood, Hb trout I and Hb trout IV, have different functional properties, which may be correlated directly with their physiological role (see ref. 1 for review). Thus, Hb trout I, which displays cooperative ligand binding at all pH values, completely lacks heterotropic interactions; on the other hand, these interactions are clearly evident in Hb trout IV, for which lowering of pH, or addition of organic phosphates, produces a large decrease in oxygen affinity and in cooperativity (n drops from 2.3 at pH 8 to ~1 at pH 6)
Giardina, B., Ascoli, F., Brunori, M., SPECTRAL CHANGES AND ALLOSTERIC TRANSITION IN TROUT HEMOGLOBIN, <<NATURE>>, 1975; 256 (5520): 761-762. [doi:10.1038/256761a0] [http://hdl.handle.net/10807/6719]
SPECTRAL CHANGES AND ALLOSTERIC TRANSITION IN TROUT HEMOGLOBIN
Giardina, Bruno;
1975
Abstract
PREVIOUS results have shown that two of the haemoglobin components from trout blood, Hb trout I and Hb trout IV, have different functional properties, which may be correlated directly with their physiological role (see ref. 1 for review). Thus, Hb trout I, which displays cooperative ligand binding at all pH values, completely lacks heterotropic interactions; on the other hand, these interactions are clearly evident in Hb trout IV, for which lowering of pH, or addition of organic phosphates, produces a large decrease in oxygen affinity and in cooperativity (n drops from 2.3 at pH 8 to ~1 at pH 6)
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