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Abstract
The extent of dissociation of various hemoglobins into subunits was estimated from their elution volumes (Ve) on G-100 Sephadex. Under the same controlled conditions carboxyhemoglobins A, A3 (A1), F, S, and C all had the same elution volumes. The carboxy and cyanmet derivatives of hemoglobin Kansas (a variant with very low oxygen affinity) had a relatively high Ve, indicating a decreased mean molecular weight and therefore an increased tendency to form dimers and even monomers. Conversely, the liganded derivatives of hemoglobin Chesapeake (a variant with high oxygen affinity) had a relatively low Ve, suggestive of an impaired degree of subunit dissociation. Deoxyhemoglobin Chesapeake had a Ve identical with that of deoxyhemoglobin A. Cat hemoglobin, known to have an unusually low oxygen affinity, was found to have a higher Ve than human, dog, rabbit, rat, or guinea pig hemoglobins.
Authors
H. Franklin Bunn
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