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. 1980 Dec;77(12):7147–7151. doi: 10.1073/pnas.77.12.7147

Kinetic study of the interaction of oxy- and deoxyhemoglobins with the erythrocyte membrane.

N Shaklai, V S Sharma
PMCID: PMC350458  PMID: 6938961

Abstract

Changes in fluorescence intensity of a membrane-embedded probe were used to study the kinetics of binding of oxy- and deoxyhemoglobin to erythrocyte membranes. For these studies, stopped-flow fluorimetric techniques were utilized. Both binding and dissociation of hemoglobin from membranes followed heterogeneous first-order kinetics. The rate constants for binding of oxyhemoglobin were about 10 times larger than those of deoxyhemoglobin; the dissociation rate constants of oxyhemoglobin were about one-quarter those of the unliganded form. The results are discussed in light of the steady-state binding constants previously derived for both oxy- and deoxyhemoglobin.

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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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