Band 4.1 enhances spectrin binding to phosphatidylserine vesicles.
Erythroid band 4.1 enhances the binding of erythroid spectrin to phosphatidylserine vesicles under conditions of ionic strength and at protein concentrations similar to those in the red cell. The extent of enhancement depends on the concentration of band 4.1; at 2 microM 4.1, spectrin binding increases approximately 10-fold (to 600 mumoles/mole lipid). The Kd is 0.5 microM, as measured by SDS-PAGE of protein-bound vesicles recovered by ficoll gradient centrifugation. The 4.1-enhanced binding of spectrin was also measured by a gel filtration assay. The electrostatic nature of the enhancement of spectrin binding is indicated by its dependence on the phosphatidylserine content of the vesicles.
Takeshita
K
K
School of Pharmaceutical Sciences, Showa University, Tokyo, Japan.
MacDonald
R I
RI
MacDonald
R C
RC
D002852:Chromatography, Ion Exchange; D003598:Cytoskeletal Proteins; D004910:Erythrocyte Membrane / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D008081:Liposomes; D008565:Membrane Proteins / Q000302:isolation & purification / Q000494:pharmacology*; D009479:Neuropeptides; D009994:Osmolar Concentration; D010713:Phosphatidylcholines / Q000378:metabolism; D010718:Phosphatidylserines / Q000378:metabolism*; D013049:Spectrin / Q000302:isolation & purification / Q000378:metabolism*
D003598:Cytoskeletal Proteins; D008081:Liposomes; D008565:Membrane Proteins; D009479:Neuropeptides; D010713:Phosphatidylcholines; D010718:Phosphatidylserines; C028841:erythrocyte membrane band 4.1 protein; C120557:erythrocyte membrane protein band 4.1-like 1; D013049:Spectrin