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Purification and Characterization of Superoxide Dismutase (SOD) from Camellia Pollen
作者姓名:HE  Xiao-hong  WU  Min  LI  Shan-yu  FAN  Hao  CHU  Yu-zhuo  LIU  Lan-ying
作者单位:[1]College of Life Science, Jilin University, Changchun 130023, P. R. China
摘    要:A superoxide dismutase( SOD ) was purified to homogeneity from fresh camellia pollen by means of ammonium sulfate precipitation and column chromatography with DEAE-cellulose( DE52 ), Sephadex G-100 and phenyl sepharose^TM 6 Fast Flow columns. Its specific activity could reach to 4034 U/mg protein and it was determined to be Cu/ Zn-SOD according to its different sensitivities to different inhibitors. The molecular weight of the SOD and its subunit were 69500 and 34700, respectively, based on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS- PAGE), which implicates that the SOD in camellia pollen is a dimmer composed of two identical subunits. The isoelectric point of the enzyme was determined to be 4. 1 by isoelectric focusing electrophoresis and the N-terminal amino acid was identified to be Gly by the DNS-Cl method. Its α-Helix was also calculated to be approximately 21.8% according to the circular dichroism(CD) spectra.

关 键 词:过氧化物  歧化酶  山茶花  花粉  净化工艺  SOD
文章编号:1005-9040(2005)-05-558-04
收稿时间:2004-11-26

Purification and Characterization of Superoxide Dismutase(SOD) from Camellia Pollen
HE Xiao-hong WU Min LI Shan-yu FAN Hao CHU Yu-zhuo LIU Lan-ying.Purification and Characterization of Superoxide Dismutase(SOD) from Camellia Pollen[J].Chemical Research in Chinese University,2005,21(5):558-561.
Authors:HE Xiao-hong  WU Min  LI Shan-yu  FAN Hao  CHU Yu-zhuo  LIU Lan-ying
Institution:College of Life Science, Jilin University, Changchun 130023, P. R. China
Abstract:A superoxide dismutase(SOD) was purified to homogeneity from fresh camellia pollen by means of ammonium sulfate precipitation and column chromatography with DEAE-cellulose(DE52), Sephadex G-100 and phenyl sepharoseTM 6 Fast Flow columns. Its specific activity could reach to 4034 U/mg protein and it was determined to be Cu/Zn-SOD according to its different sensitivities to different inhibitors. The molecular weight of the SOD and its subunit were 69500 and 34700, respectively, based on sodium dodecyl sulfate-polyacrylamide gel electrophoresis(SDS-PAGE), which implicates that the SOD in camellia pollen is a dimmer composed of two identical subunits. The iso-electric point of the enzyme was determined to be 4.1 by isoelectric focusing electrophoresis and the N-terminal amino acid was identified to be Gly by the DNS-Cl method. Its α-Helix was also calculated to be approximately 21.8% according to the circular dichroism(CD) spectra.
Keywords:Camellia pollen  Superoxide dismutase  Purification  Characterization
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