The binding of the isolated alpha-subunit of human erythrocyte spectrin to calmodulin is demonstrated by partitioning in aqueous two-phase systems. The affinity of the alpha-subunit for calmodulin is slightly higher than that of the spectrin dimer, whereas the beta-subunit interacts only very weakly. The binding is in all cases calcium-dependent and is abolished on addition of chlorpromazine. At an ionic strength close to physiological conditions, about 1 microM free calcium is required to induce maximum binding of calmodulin to spectrin dimer.
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Berglund et al. (1986) studied this question.
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