ATP-ADP exchange reaction by fragmented sarcoplasmic reticulum from bullfrog skeletal muscle.

The ATP-ADP exchange reaction and its related partial reactions of fragmented sarcoplasmic reticulum from bullfrog skeletal muscle (frog FSR) were investigated and compared with those of rabbit FSR in order to understand the characteristics of calcium-activated ATPase (Ca2+-ATPase) of frog FSR. MgATP and magnesium-free ADP are substrates for the forward and backward reaction of the ATPase activity, respectively, which is consistent with the conclusion obtained with rabbit FSR. The ATP-ADP exchange rate of frog FSR increased sharply with an increase in Ca2+ concentration up to 3 microM, and then decreased as Ca2+ concentration increased from 3 microM to 100 microM, where the level of EP continued to increase. The exchange rate of frog FSR had a value similar to the overall ATPase activity at steady state. These results contrast with observations using rabbit FSR. The exchange rate of rabbit FSR, which is 10-30 times as high as the overall ATPase activity, reached a plateau at 1 microM Ca2+, and the decrease in the exchange rate with the increase in Ca2+ concentration was not observed until the concentration was greater than 30 microM, where the plateau of the ATPase activity was maintained. These results were discussed in reference to a possible ordered reaction sequence of ATP followed by calcium in the Ca2+-ATPase reaction. It is suggested that k-5/k-6 for rabbit FSR at steady state should be larger than that for frog FSR by a factor of about 10 in the following reaction sequence. (Formula see text).