An improved procedure for the isolation of the alpha-subunit of human hemoglobin is described. The monomer-dimer equilibrium in alpha-subunit solutions has been studied by boundary analysis in gel filtration, sedimentation velocity, sedimentation equilibrium, and cross-linking with dimethyl adipimidate. A dissociation constant has been determined from the sedimentation equilibrium data. The reaction with haptoglobin of cross-linked alpha-subunit showed that the dimer fraction wound form a stable complex.
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Terpstra et al. (1976) studied this question.