Purification and characterization of superoxide dismutase(SOD) from camellia pollen

被引：0

作者：

He, XH ^{[1
]}

Wu, M ^{[1
]}

Li, SY ^{[1
]}

Fan, H ^{[1
]}

Chu, YZ ^{[1
]}

Liu, LY ^{[1
]}

机构：

[1] Jilin Univ, Coll Life Sci, Changchun 130021, Peoples R China

来源：

CHEMICAL RESEARCH IN CHINESE UNIVERSITIES | 2005年 / 21卷 / 05期

关键词：

camellia pollen; superoxide dismutase; purification; characterization;

D O I：

暂无

中图分类号：

O6 [化学];

学科分类号：

0703 ;

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 get 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 alpha-Helix was also calculated to be approximately 21.8% according to the circular dichroism ( CD) spectra.

引用

页码：558 / 561

页数：4

共 14 条

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