Abstract
The effect of Ca2+ on the stability of the Ca2+-stimulated ATPase has been investigated. Our results showed that the preincubation of the rat red cell membranes in presence of Ca2+ causes an irreversible inhibition of the enzyme. The same effect was obtained with Ba2+ instead of Ca2+. Once initiated the inactivation of the enzyme could be halted by the addition of ethylene glycol bis (B-amino ethyl ether) N,N′-tetra acitic acid (EGTA), but inactivation was irreversible. The presence of ATP in the preincubation with Ca2+ prevented the inactivation but calmodulin did not.
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