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

    Research output: Contribution to journalArticle

    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

    Fingerprint

    Chlamydomonas
    Superoxide Dismutase
    ammonium sulfate
    Purification
    homology
    homogeneity
    Isoenzymes
    chromatography
    purification
    cellulose
    isozymes
    superoxide dismutase
    gel
    fractionation
    amino acid
    enzyme
    Amino acids
    Chlamydomonas Reinhardtii
    Glycine Max
    Nicotiana plumbaginifolia

    Keywords

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

    ASJC Scopus subject areas

    • Statistics, Probability and Uncertainty
    • Applied Mathematics
    • Ecology
    • Cell Biology
    • Physiology
    • Plant Science

    Cite this

    Isozymes of superoxide dismutase in chlamydomonas and purification of one of the major isozymes containing fe. / Sakurai, Hidehiro; Kusumoto, Noriaki; Kitayama, Kaoru; Togasaki, Robert K.

    In: Plant and Cell Physiology, Vol. 34, No. 7, 10.1993, p. 1133-1137.

    Research output: Contribution to journalArticle

    Sakurai, Hidehiro ; Kusumoto, Noriaki ; Kitayama, Kaoru ; Togasaki, Robert K. / Isozymes of superoxide dismutase in chlamydomonas and purification of one of the major isozymes containing fe. In: Plant and Cell Physiology. 1993 ; Vol. 34, No. 7. pp. 1133-1137.
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    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.",
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    AU - Togasaki, Robert K.

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