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. 1980 Dec;77(12):7147-51.
doi: 10.1073/pnas.77.12.7147.

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

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

N Shaklai et al. Proc Natl Acad Sci U S A. 1980 Dec.

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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