Abstract
IN the course of experiments on the metabolism of acetylphosphate in rats, an enzyme which catalyses the hydrolysis of this substrate was found. The enzyme is present in homogenates as well as in cell-free extracts of liver, muscle, kidney, brain, but not in blood serum. Acetylphosphate M/20/20 (prepared according to Lipmann and Tuttle1) was incubated with liver homogenate and sodium bicarbonate buffer (pH 7·3) at 38° C. More than 80 per cent cleavage was observed in five minutes, and total cleavage was obtained in fifteen minutes. The spontaneous cleavage of acetylphosphate in the same conditions but in the absence of liver was 33 per cent in 180 minutes. The enzyme activity was found to be of the same order of magnitude in extracts of liver, kidney, brain and muscle.
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References
Lipmann, F., and Tuttle, L. C., J. Biol. Chem., 153, 577 (1944).
Lipmann, E., and Tuttle, L. C., J. Biol. Chem., 153, 571 (1944).
Ochoa, S., Peters, R. A., and Stocken, L. A., Nature, 144, 750 (1939).
Lipmann, F., Fed. Proc., 4, 97 (1945).
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SHAPIRO, B., WERTHEIMER, E. Acetylphosphatase in Animal Tissues. Nature 156, 690 (1945). https://doi.org/10.1038/156690a0
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DOI: https://doi.org/10.1038/156690a0
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