Abstract
Human haptoglobin (Hp) combines with hemoglobin double molecules (Hb∙Hb) isolated from an inbred strain of mice, DBA/2J. When low ionic strength solutions of the two proteins are mixed, precipitates form. The extent of precipitation is dependent upon the ratios of the two proteins in a manner similar to that seen in a classical antigen–antibody precipitin reaction. In a more alkaline buffer of higher ionic strength, complexes form which remain soluble and may be resolved as a series of bands by acrylamide disc electrophoresis. The relative concentration of each band within the series depends upon the input ratios of Hp and Hb∙Hb. These results indicate that human haptoglobin is bivalent and combines with hemoglobin in a fashion analogous to the combination of an antibody with an antigen.
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