Purification and Characterization of Superoxide Dismutase(SOD) from Camellia Pollen
Purification and Characterization of Superoxide Dismutase(SOD) from Camellia Pollen作者机构：College of Life Science Jilin University Changchun 130023 P. R. China
出 版 物：《Chemical Research in Chinese Universities》 (高等学校化学研究（英文版）)
年 卷 期：2005年第21卷第5期
页 面：558-561页
核心收录：
学科分类：081704[工学-应用化学] 07[理学] 08[工学] 0817[工学-化学工程与技术] 070303[理学-有机化学] 0703[理学-化学]
主 题：Camellia pollen Superoxide dismutase Purification Characterization
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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