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 si
ngle 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 mol
ecules. Ca2+ greatly diminished the interaction between IgG and CaM, w
ith IC50 = 8-9 mu M. These data give a novel insight into protein-prot
ein interactions.