Aggregation effects on oxygen binding of sickle cell hemoglobin.
Deoxygenation of concentrated solutions (0.33 gram per milliliter) of sickle cell hemoglobin show (i) a "crisis point" where the oxygen binding curve is unusually steep (Hill coefficient of 5 to 6), and (ii) a simultaneous increase in light scattering. Nearly identical oxygen binding curves are obtained upon oxygenation and deoxygenation of these solutions. The influence of aggregation is to shift the curve toward higher pressures.
D000494:Allosteric Regulation; D004163:Diphosphoglyceric Acids / Q000097:blood; D006451:Hemoglobin, Sickle / Q000378:metabolism*; D006801:Humans; D010100:Oxygen / Q000097:blood*; D010108:Oxyhemoglobins / Q000378:metabolism*; D012995:Solubility
D004163:Diphosphoglyceric Acids; D006451:Hemoglobin, Sickle; D010108:Oxyhemoglobins; D010100:Oxygen