Interactions of hemoglobin S with the red cell membrane.
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.
D004910:Erythrocyte Membrane / Q000378:metabolism*; D004912:Erythrocytes / Q000378:metabolism*; D006454:Hemoglobins / Q000378:metabolism*; D006801:Humans; D011485:Protein Binding; D013050:Spectrometry, Fluorescence
D006454:Hemoglobins