Properties of red cell membrane proteins: mechanism of spectrin and band 4.1 interaction.
Interactions between human red cell's band 4.1 and spectrin were studied by fluorescence resonance energy transfer and batch microcalorimetry techniques. The association constant (Ka = 8.6 X 10(7) M-1), the stoichiometry (one molecule of band 4.1 to one molecule of spectrin), the reversibility, and the enthalpy (delta H = -6 kcal/mol) were determined. A proton uptake was observed to take place as a result of the spectrin-band 4.1 complex formation. In addition to the protonation of the reaction products, the entropic contribution (-T delta S) has been observed to be responsible for approximately 50% of the binding free energy. We concluded that the environment plays a significant role in the stabilization of the complex. Since band 4.1 has been required for the maintenance of the cytoskeletal stability, small alterations of the binding energies or the degree of interaction could have a pronounced effect on the structure of the erythrocyte membrane.
D001798:Blood Proteins / Q000378:metabolism*; D003598:Cytoskeletal Proteins; D004910:Erythrocyte Membrane / Q000378:metabolism*; D005456:Fluorescent Dyes; D006801:Humans; D007700:Kinetics; D008565:Membrane Proteins / Q000097:blood*; D009479:Neuropeptides; D013049:Spectrin / Q000378:metabolism*; D013053:Spectrophotometry
D001798:Blood Proteins; D003598:Cytoskeletal Proteins; D005456:Fluorescent Dyes; D008565:Membrane Proteins; D009479:Neuropeptides; C028841:erythrocyte membrane band 4.1 protein; C120557:erythrocyte membrane protein band 4.1-like 1; D013049:Spectrin