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Abstract

The enzyme acid phosphatase was studied in Taraxacum roots with respect to its substrate and pH specificity. A pH optima of ca. 4.8 was noted after using ten different phosphate compounds as its substrate. It was found that this enzyme is actively hydrolyzing not only the sugar phosphates but also the nucleotides and coenzymes, releasing free inorganic phosphates, though the rate of the reaction differs with different

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