Abstract
Acid phosphatase F1 from <i>Avena elatior</i> 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, Zn<sup>2+</sup>, molybdate were effective inhibitors. EDTA and l, 10-phenanthroline activated the enzyme.
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