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Plant and Cell Physiology, 1985, Vol. 26, No. 7 1285-1289
© 1985

Article

Inverse Correlation of Thiol Proteinase with Nitrate Reductase Activities in Barley Leaves

Takashi Hamano1, Yoshikiyo Oji2, Saburo Okamoto2, Yukimasa Mitsuhashi1 and Yukio Matsuki1

1Public Health Research Institute of Kobe City Minatozimanaka-cho 4-6, Chuo-ku, Kobe 650, Japan
2Department of Agricultural Chemistry, Faculty of Agriculture, Kobe University Rokkodai-cho 1-1, Nada-ku, Kobe 657, Japan

Experiments conducted to determine the effects of leupeptin, a specific inhibitor of thiol proteinase, on extractable nitrate reductase (NR) activity in leaves of Hordeum distichum during darkness revealed that leupeptin (0.01 mg.ml–1) applied to detached leaves significantly reduced the loss of NR activity. At the same time it also reduced the formation of small cytochrome c reductase species, which is a degradation product of NR complex, Upon nitrate induction, extractable NR activity increased but the content of thiol proteinase decreased. This inverse correlation was also observed upon transfer of nitrate-grown barley seedlings to nitrate-free nutrient solution. Furthermore, cycloheximide (0.1 mg.ml–1) treatment of barley seedlings reduced the content of thiol proteinase and retarded the loss of NR activity under noninducing conditions. These results suggest that in vivo changes in NR content in leaves of Hordeum distichum are the result of proteolysis by an endogenous thiol proteinase.

(Received May 16, 1985; Accepted July 22, 1985)
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