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

Autor:	Irena Lorenc-Kubis, E. Wieczorek, Bronisława Morawiecka
Rok vydání:	2015
Předmět:	chemistry.chemical_classification Chromatography food.ingredient biology Chemistry Phosphatase Size-exclusion chromatography Acid phosphatase Plant Science lcsh:QK1-989 Sepharose chemistry.chemical_compound Enzyme Avena food Biochemistry Sephadex lcsh:Botany biology.protein Fluoride
Zdroj:	Acta Societatis Botanicorum Poloniae, Vol 46, Iss 3, Pp 481-488 (2015)
ISSN:	2083-9480
DOI:	10.5586/asbp.1977.038
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::da930b0f5492fad53eb651d94828f252 https://doi.org/10.5586/asbp.1977.038 Zobrazit plný text záznamu