The Binding Mechanism of Haptoglobin with Hemoglobin. II

Purification and Physico-chemical Characterization of the Intermediate and Saturated forms of Hemoglobin-haptoglobin 1-1 Complex

Abstract

The intermediate and saturated forms of human hemoglobin-haptoglobin 1-1 complex were isolated by the use of preparative acrylamide gel electrophoresis.
The average molecular weights of the intermediate and saturated complexes, estimated by the sedimentation and diffusion studies, were 135, 000 and 169, 000, respectively. From these results, it was postulated that the intermediate and saturated complexes would be resulted from the combination of one molecule of haptoglobin 1-1 protein with an αβ-subunits and/or α₂β₂(2αβ) of hemoglobin A, respectively.