Ligand kinetics of hemoglobin S containing erythrocytes.
Oxygen uptake of fully deoxygenated sickle (SS) erythrocytes is slower than that of normal (AA) erythrocytes, as demonstrated by the half-times of the overall oxygenation reactions: at 25 degrees in an isotonic phosphate buffer the normal red cells have a t1/2 = 82 +/- 4.7 msec, as compared to sickle red cells where t1/2 = 135 +/- 17.6 msec. The effects of temperature, extracellular osmolality, and the presence of an antisickling agent (n-butylurea) on the rate of red cell oxygenation strongly suggest that the differences in oxygenation rates encountered with sickle red cells is directly related to the intracellular polymerization of deoxyhemoglobin S.
D000986:Antisickling Agents / Q000494:pharmacology; D004227:Dithionite / Q000494:pharmacology; D004910:Erythrocyte Membrane / Q000378:metabolism; D004913:Erythrocytes, Abnormal / Q000378:metabolism*; D006441:Hemoglobin A / Q000378:metabolism; D006451:Hemoglobin, Sickle / Q000378:metabolism*; D006579:Heterozygote; D006801:Humans; D007700:Kinetics; D008024:Ligands; D009994:Osmolar Concentration; D010100:Oxygen / Q000378:metabolism*; D013696:Temperature; D014508:Urea / Q000031:analogs & derivatives / Q000494:pharmacology
D000986:Antisickling Agents; D006451:Hemoglobin, Sickle; D008024:Ligands; D004227:Dithionite; D014508:Urea; D006441:Hemoglobin A; C006865:butylurea; D010100:Oxygen
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