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Complex formation between gamma-immunoglobulin and calmodulin in calcium-free conditions.

We show that gamma-immunoglobulin (IgG) binds calmodulin (CaM) in a Ca(2+)-independent manner, with Kd value of (1.7 +/- 0.5) x 10(-7) M. A single IgG molecule maximally bound 10 CaM molecules. The binding is to the heavy chain or Fab portion, but not the Fc portion, of the IgG molecules. Ca2+ greatly diminished the interaction between IgG and CaM, with IC50 = 8-9 microM. These data give a novel insight into protein-protein interactions.