Subunits alpha isolated from human haptoglobin were recombined with beta subunits of equine haptoglobin, and vice versa. Both hybrid proteins were separated on electrophoresis in polyacrylamide gel into four bands with mobilities corresponding to tetramers 2alpha.2beta, trimers 2alpha.beta, and dimers alpha.beta, in addition to free subunits beta. 2. The binding ability of haemoglobin and the antigenic specificity of tetramers depended on the origin of beta subunit. 3. Reduction of native and hybrid proteins with 2-mercaptoethanol led to gradual formation of alpha.beta, alpha, and beta; the components 2alpha.beta and 2alpha appeared in trace amounts.