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- W1989492043 abstract "Acid pyrophosphatase, hydrolyzing ATP and other nucleoside triphosphates, PPi, thiamine diphosphate, and FAD, has been purified from rat liver homogenate and was separated from acid phosphatase by chromatography on CM-cellulose. ATP and PPi were hydrolyzed most rapidly at pH 5–5.4. The Km values were 0.19 mm ATP and 0.07 mm PPi. ATP was hydrolyzed to ADP, which was subsequently hydrolyzed by acid phosphatase to 5′-AMP and then to adenosine. The effects of various inhibitors and activators on the hydrolysis of ATP and PPi have been determined. The acid pyrophosphatase is not phosphoprotein phosphatase or any previously reported ATPase. Lysosomal acid pyrophosphatase, hydrolyzing ATP and PPi, was also prepared from rat kidney homogenate and further purified by chromatography on Sephadex G-200. The Km for ATP hydrolysis was 0.24 mm, and the enzyme was most active at pH 5.2–5.4. The effects of some activators and inhibitors have been determined. Some properties of acid phosphatase were studied, and a detailed study of substrate specificity was made." @default.
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- W1989492043 date "1968-01-01" @default.
- W1989492043 modified "2023-09-25" @default.
- W1989492043 title "Lysosomal acid pyrophosphatase and acid phosphatase" @default.
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- W1989492043 doi "https://doi.org/10.1016/0003-9861(68)90335-4" @default.
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