Abstract
DURING the course of an investigation of the action of vitamin K and its biological antagonists (dicoumarol, salicylate) on various phosphatases, details of which will be published elsewhere, it was observed that liver hexosediphosphatase1 exhibited a much greater sensitivity towards quinones than did the other phosphatases. Purified bone phosphomonoesterase2, for example, required a concentration of 10-3 M benzoquinone for complete inactivation, whereas 10-5 M benzoquinone was sufficient completely to inhibit the hexosediphosphatase.
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WALSH, E., WALSH, G. Inhibition of Hexosediphosphatase by Sulphhydryl Reagents and by Ascorbic Acid. Nature 161, 976–977 (1948). https://doi.org/10.1038/161976b0
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DOI: https://doi.org/10.1038/161976b0
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