Abstract
Pyruvate orthophosphate dikinase (PPDK) was detected in some C3 plants, wheat, barley, rice and tobacco, by protein blotting using an antibody against maize PPDK, although the amounts were much lesser than those of C4 plants. The PPDK activity in immature grains of rice was specifically immunoprecipitated by the anti-(maize) PPDK antibody. The molecular weight of the subunit of PPDK in all tested C3 plants was similar (ca. 95 kD) to that of maize PPDK, and the fragment patterns of the C3 PPDKs in peptide mapping were also similar to that of maize PPDK. These results suggest that C3 PPDKs have a primary structure similar to that of maize PPDK. In order to obtain information about the expression of PPDK in C3 plants, changes in the enzyme activity and in the amount of PPDK protein were investigated during the greening of rice seedlings. PPDK, which was found in the etiolated seedlings, decreased temporarily in an early stage of greening and then increased. The mechanism of this variation is discussed.
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