THE NUMBER OF SUBUNITS IN THE MOLECULE OF HORSE HEMOGLOBIN

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Abstract
The molecular weights of horse hemoglobin, horse globin, and performic acid oxidized horse globin were determined by osmotic pressure, by an approach to equilibrium sedimentation, and by light scattering (except hemoglobin) at pH 1.5 to 2.5 in 0.05 M NaCl. Sedimentation coefficients were determined for these materials over the same pH range and electrophoretic analyses were made from pH 1.5 to 4.0. The results show that in dilute salt solutions below pH 2.5 horse hemoglobin dissociates to four subunits all approximately equal in mass but at least two of which differ electrokinetically and therefore in composition. The subunits are probably held together in the native hemoglobin molecule only by non-covalent bonds.