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. 1981 Jan;78(1):65–68. doi: 10.1073/pnas.78.1.65

Interaction of sickle cell hemoglobin with erythrocyte membranes.

N Shaklai, V S Sharma, H M Ranney
PMCID: PMC318990  PMID: 6941263

Abstract

The interactions of hemoglobin S with the erythrocyte membrane were compared with the corresponding interactions of hemoglobin A by measuring in both steady-state and kinetic experiments the quenching of the fluorescence of a probe embedded in erythrocyte membranes. Whereas hemoglobin A could be dissociated from membranes, a fraction of hemoglobin S was irreversibly bound even in the oxy state. Deoxyhemoglobin S interacted much more strongly with erythrocyte membranes than did deoxyhemoglobin A: a portion of the deoxyhemoglobin S was irreversibly bound, and the reversibly bound fraction of hemoglobin S dissociated more slowly than did deoxyhemoglobin A. It is suggested that the binding of deoxyhemoglobin S is a two-step reaction in which the first step involves electrostatic interaction with band III erythrocyte membrane protein and the second step involves a hydrophobic interaction with membrane lipids. The latter reaction reflects the greater hydrophobicity of hemoglobin S. The unique interaction of hemoglobin S with erythrocyte membranes may be important in the formation of irreversibly sickled cells.

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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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