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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1977 Jan;74(1):203–206. doi: 10.1073/pnas.74.1.203

Ligand kinetics of hemoglobin S containing erythrocytes.

J P Harrington, D Elbaum, R M Bookchin, J B Wittenberg, R L Nagel
PMCID: PMC393226  PMID: 264675

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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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