Abnormal precipitation of oxyhemoglobin S by mechanical shaking.
The oxy-form of sickle hemoglobin (Hb S) is abnormally unstable and precipitates at a 10-fold faster rate than does oxyhemoglobin A (oxy-Hb A) during mechanical shaking. The apparent rate of precipitation of heterozygous hemolysate (AS) is approximately half that of oxy-Hb S. The deoxy-form of Hb S, on the other hand, is resistant to the mechanical treatment. This stabilization is attributed to the conformational change of hemoglobin rather than the lack of oxygen, because carbonmonoxide hemoglobin S, which is known to have conformational properties similar to those of oxy-Hb, is unstable even under anaerobic conditions. Methemoglobin S is most unstable, although addition of cyanide stabilizes the protein. The precipitation of oxy-Hb S is inhibited by ethanol and other organic solvents. The relationship of the mechanical instability of sickle oxyhemoglobin to intraerythrocytic denaturation and vaso-occlusive phenomena in sickle cell disease to be determined.
D002021:Buffers; D055598:Chemical Phenomena; D011232:Chemical Precipitation; D002621:Chemistry; D000431:Ethanol; D005292:Ferricyanides; D006454:Hemoglobins; D006455:Hemoglobins, Abnormal; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007659:Ketones; D008024:Ligands; D010100:Oxygen; D010108:Oxyhemoglobins; D011188:Potassium; D011487:Protein Conformation; D011489:Protein Denaturation; D013057:Spectrum Analysis; D013696:Temperature; D014732:Vibration
D002021:Buffers; D005292:Ferricyanides; D006454:Hemoglobins; D006455:Hemoglobins, Abnormal; D007659:Ketones; D008024:Ligands; D010108:Oxyhemoglobins; D000431:Ethanol; D011188:Potassium; D010100:Oxygen