Interaction of hemoglobin with red blood cell membranes as shown by a fluorescent chromophore.
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 Förster formulation, the quantitative data for the binding were derived. The number of binding sites was found to be 1.4 +/- 0.2 X 10(6) molecules per cell and the binding constant was 0.85 X 10(8) M-1.
D004735:Energy Transfer; D004910:Erythrocyte Membrane / Q000648:ultrastructure*; D004912:Erythrocytes / Q000648:ultrastructure*; D005456:Fluorescent Dyes; D006454:Hemoglobins; D006801:Humans; D007700:Kinetics; D008274:Magnesium; D008433:Mathematics; D009994:Osmolar Concentration; D011485:Protein Binding; D013050:Spectrometry, Fluorescence
D005456:Fluorescent Dyes; D006454:Hemoglobins; D008274:Magnesium