Open AccessPhosphatase activity of Poa pratensis seeds. I. Preliminary studies on acid phosphatase II
Author(s) -
Irena LorencKubis,
Bronisława 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