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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
. 1973 May;70(5):1506–1508. doi: 10.1073/pnas.70.5.1506

Concerted Formation of the Gel of Hemoglobin S

Robley C Williams Jr 1
PMCID: PMC433530  PMID: 4514319

Abstract

Apparent weight-average molecular weights of hemoglobin A and hemoglobin S were measured at high concentrations by equilibrium ultracentrifugation. Carbonmonoxy-hemoglobin S appears to exist as a solution of unassociated molecules, as do carbonmonoxy-and deoxy-hemoglobin A. Deoxy-hemoglobin S, however, exists in a gel-like state at concentrations above 14 g/dl, but no aggregates smaller than the gel were observed in solutions that were in equilibrium with the gel. Carbamoylation of hemoglobin S produced a solution of unaggregated molecules, as did cooling of uncarbamoylated hemoglobin S to 5°. It is concluded that the gel of hemoglobin S is formed in a stoichiometrically concerted manner, and that the size of the smallest stable aggregate is greater than 20 hemoglobin molecules.

Keywords: hemoglobin A, sickle-cell anemia, ultracentrifugation, protein association

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Selected References

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