Classification and localization of hemoglobin binding sites on the red cell membrane

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Abstract
The binding of Hb to the red cell membrane [human] was characterized over a wide range of free Hb concentrations by measurement of membrane bound and supernatant Hb. Scatchard analysis of the binding data revealed 2 classes of sites: high affinity sites with a binding constant of 1 .times. 108 M-1 and 1.2 .times. 106 sites per cell, and a 2nd, low affinity class of sites with a binding constant of 6 .times. 106 M-1 and 6 .times. 106 sites per cell. The low affinity sites are nonspecific and appear to be a result of the ghost preparation. The high affinity sites are specific to the inner surface of the red cell membrane. The competition of Hb and glyceraldehyde-3-phosphate dehydrogenase suggests band III proteins as a potential binding site for Hb.

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