Phosphatase activity of Poa pratensis seeds. I. Preliminary studies on acid phosphatase II
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Acid phosphatase (EC 3.1.3.2) was extracted with 0.1 M sodium acetate buffer pH 5.1 from <i>Poa pratensis</i> seeds, and separated into three fractions by chromatography on DEAE cellulose. The highest activity was found in fraction Il-b (acid phosphatase II). The activity of the enzyme was optimal at pH 4.9. It hydrolyzed p-nitrophenyl phosphate most readily among the various phosphomonoesters examined. Acid phosphatase II showed also a high activity toward β-naphtyl phosphate and phenyl phosphate, very low activity towards β-glycero phosphate, 5'-GMP and no activity with glucose-1 phosphate. The enzyme was inhibited by Ca<sup>2+</sup> and fluoride, but activated by Mg<sup>2+</sup>. EDTA had no influence on the activity of the enzyme.
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