Interaction of hemoglobin with band 3: a review.
The oxygen transport protein hemoglobin interacts specifically and reversibly with the red cell membrane. pH and ionic strength dependence of these interactions indicate their electrostatic nature. The anion transport protein band 3 has been implicated as the protein to which hemoglobin binds. Hemoglobin, aldolase and glyceraldehyde 3-phosphate dehydrogenase have a similar pH and ionic strength dependence in binding to 23K fragment. The three compete for the same amino-terminal 23 residue sequence region of band 3. The binding site is a highly acidic segment without any positive charge. We have recently determined the sequence of amino-terminal 23K fragment of band 3. There is a remarkable internal sequence homology between the first eleven and next eleven residues in this sequence region. Biophysical measurements in this sequence region. Biophysical measurements have revealed that 23K is a tetramer under physiological conditions. The implications of this structure of 23K is discussed with respect to the interaction of band 3 with the red cell cytoskeleton.
D000595:Amino Acid Sequence; D001457:Anion Exchange Protein 1, Erythrocyte / Q000032:analysis / Q000378:metabolism*; D001665:Binding Sites; D001667:Binding, Competitive; D004910:Erythrocyte Membrane / Q000378:metabolism; D005634:Fructose-Bisphosphate Aldolase / Q000097:blood; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000097:blood; D006454:Hemoglobins / Q000378:metabolism*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D009994:Osmolar Concentration
D001457:Anion Exchange Protein 1, Erythrocyte; D006454:Hemoglobins; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D005634:Fructose-Bisphosphate Aldolase