Purification and properties of acid phosphatase from Avena elatior L. seeds | Zendy

E. Wieczorek | Zendy; Irena LorencKubis | Zendy; B Morawiecka | Zendy

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Purification and properties of acid phosphatase from Avena elatior L. seeds

Author(s) -

E. Wieczorek,

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.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

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