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Ligand Kinetics of Hemoglobin S Containing Erythrocytes

John P. Harrington, Danek Elbaum, Robert M. Bookchin, Jonathan B. Wittenberg and Ronald L. Nagel
Proceedings of the National Academy of Sciences of the United States of America
Vol. 74, No. 1 (Jan., 1977), pp. 203-206
Stable URL: http://www.jstor.org/stable/66543
Page Count: 4
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Ligand Kinetics of Hemoglobin S Containing Erythrocytes
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Abstract

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.

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