Abstract
An acid phosphatase from yam tuber cytoplasm has been purified by ammonium sulfate fractionation, ion exchange chromatography through CM-Sephadex A-50 and gel filtration through Sephadex G-200. The preparation was homogeneous by polyacrylamide gel electrophoresis and has an apparent molecular weight of 98 000 ± 2000. This enzyme shows no effects towards phosphorylated sugars and appears to hydrolyze adenosine-2′,5′-diphosphate, adenosine-3′,5′-monophosphate as natural metabolites are concerned. The enzymatic activity was inhibited by Ca 2+, Hg 2+ and particularly increased by Mg 2+. This effect and the inhibition by EDTA are in favor of metalloprotein nature of this enzyme.
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