Glutathione reductase (GR) was purified from spinach leaves to the homogeneous state, based on native- and SDS-PAGE bindings. The GR had a polypeptide of 60 kilodalton and its absorption spectrum was similar to that of GR from human erythrocytes. Antibody against spinach GR, prepared from rabbit, inhibited GR activity, while the non-immune serum had no effect on the enzyme activity. Purified enzyme and crude extracts from spinach leaves produced fused precipitin lines with anti-GR on the Ouchterlony double diffusion tests. Although crude extracts from tobacco and petunia leaves reacted with anti-GR, these precipitin lines fused only partially with the line between purified spinach GR and anti-spinach GR. Moss, fern and Chlorella crude extracts and purified yeast GR produced no precipitin lines with anti-spinach GR. The extractable GR activity increased significantly in 0.07 ppm O3-fumigated spinach leaves, whereas they suffered no visible injuries. The results from the immunoblotting method confirmed that the O3-induced increase in extractable GR activity is due to an increase in the protein level of GR.
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Tanaka et al. (1988) studied this question.