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    The Effect of DPG and IHP on the Relative Thermodynamic Affinity for CO of the Subunits of Rabbit Hemoglobin

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    The two chains of most hemoglobins interact differently with ligands as can be seen in two nmr resonances for bound ^(13)CO (Moon and Richards, 1972). This observation has led to interest in the possibility that the two chains have different thermodynamic affinities toward ligands (Huestis and Raftery, 1973, 1975; Moon and Richards, 1974; Huang and Redfield, 1976; Viggiano and Ho, 1979a,b). Rabbit hemoglobin possesses an unusual α-chain which causes ^(13)CO bound to it to have a different chemical shift than ^(13)CO bound to β chains (Moon and Richards, 1972, 1974) and, thereby, allows direct quantitative observation of the degree of ligation of the two subunits
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