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• W2050295087 abstract "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." @default.
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• W2050295087 date "1981-01-01" @default.
• W2050295087 modified "2023-10-15" @default.
• W2050295087 title "Spectrin oligomers: A structural feature of the erythrocyte cytoskeleton" @default.
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• W2050295087 doi "https://doi.org/10.1002/jsscb.380170308" @default.
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