Isozymes of superoxide dismutase in chlamydomonas and purification of one of the major isozymes containing fe

Hidehiro Sakurai*, Noriaki Kusumoto, Kaoru Kitayama, Robert K. Togasaki

*この研究の対応する著者

研究成果: Article査読

10 被引用数 (Scopus)

抄録

Electrophoretic analysis of Chlamydomonas reinhardtii extract revealed at least 4 distinct superoxide dismutase (SOD) activity bands as well as several additional minor bands. Among them, one was deduced to be Fe-type and the other three Mn-type based on their susceptibility to KCN and H2O2. The Fe-SOD, which occupied about 40% of the total soluble activity, was purified to homogeneity using ammonium sulfate fractionation followed by DEAE-cellulose, hydroxyapatite, and Superdex 75 gel-permeation chromatography. The 40-kDa native enzyme was composed of two identical 20-kDa subunits with a low shoulder of absorption at ̃350 nm. The NH2-terminal amino acid sequence determined up to residue 29 showed a high homology to those of Fe-SOD from Arabidopsis thaliana, Glycine max, and Nicotiana plumbaginifolia.

本文言語English
ページ(範囲)1133-1137
ページ数5
ジャーナルPlant and Cell Physiology
34
7
出版ステータスPublished - 1993 10

ASJC Scopus subject areas

  • 生理学
  • 植物科学
  • 細胞生物学

フィンガープリント

「Isozymes of superoxide dismutase in chlamydomonas and purification of one of the major isozymes containing fe」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。

引用スタイル