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Published on: February 7, 2013
Interactions of hemoglobin S with the red cell membrane
Abstract:
Significant differences were observed in the binding of hemoglobin A and hemoglobin S to normal red cell membranes containing the fluorescent chromophore 12-(9-anthroyl) stearic acid. Deoxyhemoglobin S had a greater affinity for the membrane than did deoxyhemoglobin A and part of the binding of deoxyhemoglobin S appeared to be irreversible. When the hemoglobin binding site in red cell membranes, Band 3, was blocked with with glyceraldehyde-3-phosphate dehydrogenase, neither hemoglobin S nor A was bound. It is suggested that the binding sites for hemoglobin S to normal red cell membranes involves two steps: (1) the binding of hemoglobin to Band 3 in which increased binding reflects the greater positive charge followed by (2) a component of irreversible binding, believed to reflect an interaction between a hydrophobic area of hemoglobin S and red cell lipids.
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