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Isolation and characterization of an iron-containing superoxide dismutasefrom Lycium chinense fruit

Cheng Guangyu, Wei Jincheng, Wu Guorong, Liu Zilie, Zou Yuzhen

Department of Biology, Nanjing Normal University, Nanjing,Jiangsu

Abstract

Iron-containing superoxide dismutase was found in the crude extract fromfruit of Lycium chinense Mill, the enzyme was isolated and purified tohomogeneity by ammonium sulfate fractionation, DEAE-Sephadex A-50chromatography and Sephadex G-100 gel filtration. The enzyme had a specificactivity of about 1000U/mg, and exhibited one absorption maximum in theultraviolet at 278nm. The purified enzyme was stable up to at least 65℃. Theenzyme activity could be inhibited by H_(2)O_(2) but was unaffected byKCN. The enzyme has a relative molecular mass of about 44.6kD and is composedof two equal subunits. The molecular mass of the subunits has been found to be22.0kD. The Fe-enzyme contains about 1 gram atom of Fe per dimer and containsmore glycine residues than the Fe-SOD from procaryotes and other eucaryotes.

Key words: Lycium chinense Mill;Iron-containing superoxide dismutase;Fruit;Purification;Property

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Citing This Article：

Cheng Guangyu, Wei Jincheng, Wu Guorong, Liu Zilie, Zou Yuzhen. Isolation and characterization of an iron-containing superoxide dismutasefrom Lycium chinense fruit. Acta Physiol Sin 1994; 46 (2): (in Chinese with English abstract).