Spectrin oligomers: a structural feature of the erythrocyte cytoskeleton.
Spectrin reversibly self-associates to high molecular weight oligomers through a concentration-driven process characterized by association constants of about 10(5) mol(-1). This association if prominent under physiological conditions of pH, ionic strength, and temperature. It is disrupted by urea, but not Triton X-100. The process of spectrin association appears mathematically to resemble that for tropomyosin, although the mechanism is probably different. Spectrin association is weak compared to other prominent protein-protein associations in the red cell membrane skeleton. The linkage of these weak and strong associations suggests a process whereby the membrane skeleton spontaneously assembles. Such affinity-modulated assembly involving weak associations is likely to abe the focus of numerous membrane.
D003902:Detergents; D004910:Erythrocyte Membrane / Q000648:ultrastructure*; D004912:Erythrocytes / Q000648:ultrastructure*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D046911:Macromolecular Substances; D008565:Membrane Proteins; D008970:Molecular Weight; D017830:Octoxynol; D009994:Osmolar Concentration; D011092:Polyethylene Glycols; D013049:Spectrin; D013696:Temperature; D014508:Urea
D003902:Detergents; D046911:Macromolecular Substances; D008565:Membrane Proteins; D013049:Spectrin; D011092:Polyethylene Glycols; D014508:Urea; D017830:Octoxynol