The preparation of human hemoglobin α-subunit and a study of its monomer–dimer association

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Abstract
An improved procedure for the isolation of the .alpha.-subunit of human Hb is described. The monomer-dimer equilibrium in .alpha.-subunit solutions was studied by boundary analysis in gel filtration, sedimentation velocity, sedimentation equilibrium and cross-linking with dimethyl adipimidate. A dissociation constant was determined from the sedimentation equilibrium data. The reaction with haptoglobin of cross-linked .alpha.-subunit showed that the dimer fraction would form a stable complex.