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

E. Wieczorek, I. Lorenc-Kubis, B. Morawiecka


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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DOI: https://doi.org/10.5586/asbp.1977.038

Journal ISSN:
  • 2083-9480 (online)
  • 0001-6977 (print; ceased since 2016)
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