Does Ternary Complex Formation Control the State of the Cation Barrier in the Resealed Human Red Blood Cell Ghost?

The permeability properties of the resealed ghost membrane depend on the pH at hemolysis. If resealed ghosts are prepared by hypotonic hemolysis at 0°C, pH 6.0 with maximal dilution of endogenous chelators, resealing for Na and K takes place when a new pool of chelators is supplied. However, when prepared by hemolysis at pH 7.6 or above, the cation barrier cannot be restored. A model is suggested where ternary complex formation between an endogenous chelator, Ca and a membrane site control the state of the cation barrier