Glutamate synthase isoforms in tobacco nicotiana tabacum cultivar xanthi

Suzuki, A.; Nato, A.; Gadal, P.

Plant Science Letters 33(1): 93-102

1984


Accession: 005528756

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Abstract
Glutamate synthase in tobacco cultured cells was assayed with different electron donors upon greening of etiolated cells. Ferredoxin-dependent glutamate synthase (EC 1.4.7.1) activity increased 4-fold, whereas NADH-dependent glutamate synthase (EC 1.4.1.14) and NADPH-dependent glutamate synthase (EC 1.4.1.13) activities remained constant during greening of the cells. Ferredoxin-dependent glutamate synthase and NAD(P)H-dependent glutamate synthases were distinguished by their chromatographic behavior on ferredoxin-Sepharose affinity column. The immunoglobulin G (IgG)-anti-ferredoxin-dependent glutamate synthase from rice green leaves cross-reacted with ferredoxin-dependent glutamate synthase, but NAD(P)H-dependent glutamate synthases were not immunoprecipitated with the IgG, indicating that ferredoxin-dependent glutamate synthase NAD(P)H-dependent glutamate synthase activities are carried out by distinct protein molecules in tobacco cultured cells. Some physiological functions of the enzymes are discussed.