Open AccessPurification and properties of acid phosphatase from Avena elatior L. seeds
Author(s) -
E. Wieczorek,
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.1977.038
Subject(s) - sephadex , avena , chemistry , acid phosphatase , enzyme , phosphatase , size exclusion chromatography , chromatography , column chromatography , molybdate , biochemistry , biology , botany , organic chemistry
Acid phosphatase F1 from Avena elatior seeds was isolated and partially purified by means of alcohol precepitation, DEAE-, CM-column chromatography, Sephadex G-150, Sephadex G-200 and Sepharose 4B - gel filtration. The enzyme was stable at 50°C, pH 5.1. The pH optimum for phosphatase activity was 4.2. Fluoride, Zn2+, molybdate were effective inhibitors. EDTA and l, 10-phenanthroline activated the enzyme