| Literature DB >> 6941263 |
N Shaklai, V S Sharma, H M Ranney.
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.Mesh：
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Year: 1981 PMID： 6941263 PMCID： PMC318990 DOI： 10.1073/pnas.78.1.65
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205