Abstract
A double mixing stopped-flow method is described for studying the dimer-tetramer equilibria of oxyhemoglobins and the kinetics of association of unliganded dimers. The three hemoglobins studied were: Hb Carp, Hb A, and Hb Rothschild (Trp β37(C3) → Arg). The new method reproduces the data obtained for oxyHb A by other established methods. In agreement with previous studies, the new method indicates little, if any, dissociation of oxyHb carp into dimers even in 2 m urea solutions (0.1 m Bis-Tris pH 7.0). OxyHb Rothschild, on the other hand, is extensively dissociated into dimers ( K(Hb 4L 4 lrhar2 2Hb 2) = 37.3 × 10 −6 m) and the rate constant for the association of deoxy dimers of Hb Rothschild is about one-tenth of the value for Hb A indicating that the deoxy tetramer of Hb Rothschild is at least 10 times more dissociated into dimers than deoxyHb A.
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