Ligand kinetics of hemoglobin S containing erythrocytes.

Abstract
O2 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.degree. C in an isotonic phosphate buffer, the normal red cells have a t 1/2 = 82 .+-. 4.7 ms, as compared to sickle red cells where t 1/2 = 135 .+-. 17.6 ms. 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 deoxyHb S.