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- W295258575 abstract "This chapter discusses adenosine triphosphate (ATP) hydrolysis with CaATP as a substrate to obtain information about the role of divalent cation in ATP hydrolysis. The existence and properties of this type of ATP hydrolysis have not so far been established. The results indicated that the ATPase can turn over normally with CaATP as a substratebut at a very slow rate. Mg2+ was not required for the turnover of the ATPase per se. Sarcoplasmic reticulum (SR) vesicles were prepared from rabbit skeletal muscle. The amount of calcium bound to the ATPase was measured by a membrane filtration method. At appropriate intervals after the addition of EDTA to the reaction mixture, 0.1 ml of the reaction mixture was rapidly passed through a membrane filter (HA 0.45-Um Millipore filter) by suction at 2°C. Then, the membrane filter was washed three times with 2 ml of a solution containing imidazole/HCl (pH 7.0) and EDTA, the concentrations of which were the same as those in the reaction mixture." @default.
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- W295258575 date "1985-01-01" @default.
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- W295258575 title "REACTION MECHANISM OF ATP HYDROLYSIS BY SARCOPLASMIC RETICULUM WITH CaATP AS A SUBSTRATE" @default.
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- W295258575 doi "https://doi.org/10.1016/b978-0-12-260380-8.50027-0" @default.
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