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

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

School of Education

Research output: Contribution to journal › Article

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 language	English
Pages (from-to)	1133-1137
Number of pages	5
Journal	Plant and Cell Physiology
Volume	34
Issue number	7
Publication status	Published - 1993 Oct 1

Keywords

Amino acid sequence
Chlamydomonas reinhardtii
Fe-SOD
Superoxide dismutase

ASJC Scopus subject areas

Physiology
Plant Science
Cell Biology

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Sakurai, H., Kusumoto, N., Kitayama, K., & Togasaki, R. K. (1993). Isozymes of superoxide dismutase in chlamydomonas and purification of one of the major isozymes containing fe. Plant and Cell Physiology, 34(7), 1133-1137.

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title = "Isozymes of superoxide dismutase in chlamydomonas and purification of one of the major isozymes containing fe",

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.",

keywords = "Amino acid sequence, Chlamydomonas reinhardtii, Fe-SOD, Superoxide dismutase",

author = "Hidehiro Sakurai and Noriaki Kusumoto and Kaoru Kitayama and Togasaki, {Robert K.}",

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T1 - Isozymes of superoxide dismutase in chlamydomonas and purification of one of the major isozymes containing fe

AU - Sakurai, Hidehiro

AU - Kusumoto, Noriaki

AU - Kitayama, Kaoru

AU - Togasaki, Robert K.

PY - 1993/10/1

Y1 - 1993/10/1

N2 - 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.

AB - 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.

KW - Amino acid sequence

KW - Chlamydomonas reinhardtii

KW - Fe-SOD

KW - Superoxide dismutase

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