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

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10 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)1133-1137
Number of pages5
JournalPlant and Cell Physiology
Volume34
Issue number7
Publication statusPublished - 1993 Oct 1

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Keywords

  • Amino acid sequence
  • Chlamydomonas reinhardtii
  • Fe-SOD
  • Superoxide dismutase

ASJC Scopus subject areas

  • Physiology
  • Plant Science
  • Cell Biology

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