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)2,3.
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GIARDINA, B., ASCOLI, F. & BRUNORI, M. Spectral changes and allosteric transition in trout haemoglobin. Nature 256, 761–762 (1975). https://doi.org/10.1038/256761a0
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DOI: https://doi.org/10.1038/256761a0
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