Interaction of Hemoglobin with Red Blood Cell Membranes as Shown by a Fluorescent Chromophore

Nurith Shaklai; Helen M. Ranney; Juan Yguerabide

doi:10.1021/bi00644a031

Interaction of Hemoglobin with Red Blood Cell Membranes as Shown by a Fluorescent Chromophore

Nurith Shaklai, Helen M. Ranney, Juan Yguerabide

Research output: Contribution to journal › Article › peer-review

Abstract

Hemoglobin quenching of the fluorescence intensity of 12-(9-anthroyl)stearic acid (AS) embedded in the red blood cell membrane occurs through an energy transfer mechanism and can be used to measure the binding of hemoglobin to the membrane. The binding of hemoglobin to red cell membranes was found to be reversible and electrostatic in nature. Using a theory of energy transfer based on Forster formulation, the quantitative data for the binding were derived. The number of binding sites was found to be 1.4 ± 0.2 × 10⁶ molecules per cell and the binding constant was 0.85 × 10⁸ M^-1.

Original language	English
Pages (from-to)	5585-5592
Number of pages	8
Journal	Biochemistry
Volume	16
Issue number	25
DOIs	https://doi.org/10.1021/bi00644a031
State	Published - 1 Dec 1977
Externally published	Yes

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abstract = "Hemoglobin quenching of the fluorescence intensity of 12-(9-anthroyl)stearic acid (AS) embedded in the red blood cell membrane occurs through an energy transfer mechanism and can be used to measure the binding of hemoglobin to the membrane. The binding of hemoglobin to red cell membranes was found to be reversible and electrostatic in nature. Using a theory of energy transfer based on Forster formulation, the quantitative data for the binding were derived. The number of binding sites was found to be 1.4 ± 0.2 × 106 molecules per cell and the binding constant was 0.85 × 108 M-1.",

author = "Nurith Shaklai and Ranney, {Helen M.} and Juan Yguerabide",

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AU - Ranney, Helen M.

AU - Yguerabide, Juan

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Y1 - 1977/12/1

N2 - Hemoglobin quenching of the fluorescence intensity of 12-(9-anthroyl)stearic acid (AS) embedded in the red blood cell membrane occurs through an energy transfer mechanism and can be used to measure the binding of hemoglobin to the membrane. The binding of hemoglobin to red cell membranes was found to be reversible and electrostatic in nature. Using a theory of energy transfer based on Forster formulation, the quantitative data for the binding were derived. The number of binding sites was found to be 1.4 ± 0.2 × 106 molecules per cell and the binding constant was 0.85 × 108 M-1.

AB - Hemoglobin quenching of the fluorescence intensity of 12-(9-anthroyl)stearic acid (AS) embedded in the red blood cell membrane occurs through an energy transfer mechanism and can be used to measure the binding of hemoglobin to the membrane. The binding of hemoglobin to red cell membranes was found to be reversible and electrostatic in nature. Using a theory of energy transfer based on Forster formulation, the quantitative data for the binding were derived. The number of binding sites was found to be 1.4 ± 0.2 × 106 molecules per cell and the binding constant was 0.85 × 108 M-1.

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Interaction of Hemoglobin with Red Blood Cell Membranes as Shown by a Fluorescent Chromophore

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