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- W2087434802 abstract "A manual ATPase assay which measures the release of 32Pi from [γ-32P]ATP is described. Sodium dodecyl sulfate is used to terminate the enzyme reaction and extraction of the phophomolybdate complex into xylene: isobutanol is used to separate 32Pi from [γ-32P]ATP for quantitation by scintillation counting. The three-step assay is rapid (75–90 samples/h) and minimizes hydrolysis of ATP due to exposure to acidie conditions. The extraction procedure separates 10−15 to 10−7 mol of 32Pi from aqueous solution with an efficiency of 100,7 ± 0.62%. Less than 1% of unhydrolyzed [γ-32P]ATP is extracted. Extraction efficiency is not affected by protein or salts commonly present in enzyme incubation mixtures. Results obtained with this assay are precise, with an intraassay coefficient of variation of 0.6% and an interassay coefficient of variation of 1.8%. The results are comparable to results obtained with a spectrophotometric assay, with a correlation coefficient of 0,996, though assay performance and sensitivity are greatly improved with the isotopic assay." @default.
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- W2087434802 date "1978-10-01" @default.
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- W2087434802 title "A sensitive and precise isotopic assay of ATPase activity" @default.
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- W2087434802 doi "https://doi.org/10.1016/0003-2697(78)90169-0" @default.
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