Vigna radiata (mung bean) acid phosphatase is difficult to purify and may have a role as a vegetative Storage protein

Acid phosphatase from mung bean (Vigna radiata) germinated seeds was partially purified via ammonium sulfate precipitation and fully purified via gel excision and heat denaturation, yielding a 29 kDa protein. Using 4-nitrophenylphosphate as a substrate, Vmax and Km values of 0.10 µmol/min and 0.27 mM, respectively, were obtained. The acid phosphatase was heat resistant, enhanced by the presence of Fe2+ and Mn2+ salts, and inhibited by the...