Immunological Properties of Spinach Glutathione Reductase and Inductive Biosynthesis of the Enzyme with Ozone

概要

論文の詳細を見る
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 f-used 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 O_3-fumigated spinach leaves, whereas they suffered no visible injuries. The results from the immunoblotting method confirmed that the O_3-induced increase in extractable GR activity is due to an increase in the protein level of GR.
日本植物生理学会の論文