| Purification and Characterization of Superoxide Dismutase （SOD） from Camellia Pollen |
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| 引用本文： | 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]. 高等学校化学研究, 2005, 21(5): 558-561 |
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| 作者姓名： | HE Xiao-hong WU Min LI Shan-yu FAN Hao CHU Yu-zhuo LIU Lan-ying |
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| 作者单位： | [1]College of Life Science, Jilin University, Changchun 130023, P. R. China |
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| 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.
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| 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 |
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| 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 |
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| Authors: | HE Xiao-hong WU Min LI Shan-yu FAN Hao CHU Yu-zhuo LIU Lan-ying |
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| Affiliation: | College of Life Science, Jilin University, Changchun 130023, P. R. China |
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| 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. |
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| Keywords: | Camellia pollen Superoxide dismutase Purification Characterization |
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