Phosphatase activity of Poa pratensis seeds. I. Preliminary studies on acid phosphatase II | Zendy

Irena LorencKubis | Zendy; B Morawiecka | Zendy

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Phosphatase activity of Poa pratensis seeds. I. Preliminary studies on acid phosphatase II

Author(s) -

Irena LorencKubis,

B Morawiecka

Publication year - 2015

Publication title -

acta societatis botanicorum poloniae

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.297

H-Index - 29

eISSN - 2083-9480

pISSN - 0001-6977

DOI - 10.5586/asbp.1973.028

Subject(s) - phosphomonoesters , acid phosphatase , chemistry , phosphate , phosphatase , enzyme , hydrolysis , poa pratensis , enzyme assay , biochemistry , sodium acetate , specific activity , chromatography , biology , inorganic phosphate , poaceae , botany

Acid phosphatase (EC 3.1.3.2) was extracted with 0.1 M sodium acetate buffer pH 5.1 from Poa pratensis 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 Ca2+ and fluoride, but activated by Mg2+. EDTA had no influence on the activity of the enzyme

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