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Plant and Cell Physiology, 1993, Vol. 34, No. 7 1133-1137
© 1993

Short Communication

Isozymes of Superoxide Dismutase in Chlamydomonas and Purification of One of the Major Isozymes Containing Fe

Hidehiro Sakurai1, Noriaki Kusumoto1, Kaoru Kitayama2 and Robert K. Togasaki2

1Department of Biology, School of Education, Waseda University Nishiwaseda, Shinjuku, Tokyo, 169-50 Japan
2Department of Biology, Indiana University Bloomington, IN 47405, U.S.A.

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 {small tilde}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.

(Received December 21, 1992; Accepted May 28, 1993)
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