Affinity of heavy metal ions to intracellular Ca2+-binding proteins.

Parvalbumin, troponin C and vitamin D dependent Ca2+-binding proteins (CaBP type I and II) share the property of calmodulin to interact with some heavy metal ions. In flow dialysis and in spot tests the affinities of Cd2+ and Pb2+ to these proteins were comparable to those of Ca2+. The relative affinities were for calmodulin: Pb2+ greater than Ca2+ greater than Cd2+, for troponin C: Ca2+ greater than Cd2+ greater than Pb2+, for CaBP I: Ca2+ approximately Pb2+, for CaBP II; Ca2+ greater than Pb2+ greater than Cd2+, and for parvalbumin: Cd2+ approximately Ca2+ greater than Pb2+. Upon gel filtration of the supernatant of a pig mucosal homogenate, binding for both Pb2+ and Ca2+ appeared in the MW range of 10,000, together with CaBP II. We conclude that the investigated proteins bind heavy metal ions, in particular Pb2+ and Cd2+, similar to calmodulin. Their role in transport, storage and toxicity remains to be assessed.