Plant Physiol. Drug Metab Dispos
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Plant Physiology 70:827-832 (1982)
© 1982 American Society of Plant Biologists

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Articles

Glutamate Synthase Isoforms in Rice

Immunological Studies of Enzymes in Green Leaf, Etiolated Leaf, and Root Tissues

Akira Suzuki1, Jean Vidal and Pierre Gadal

Laboratoire de Physiologie Végétale Métabolique, ERA au CNRS 799, Université de Paris-Sud, Centre d'Orsay, Bâtiment 430, 91405 Orsay Cedex, France

Rabbit antiserum was raised against ferredoxin-dependent glutamate synthase (EC 1.4.7.1) purified from green leaves of Oryza sativa L. cv Delta. Ferredoxin-dependent glutamate synthase, detected in green leaf, etiolated leaf, and root tissues cross-reacted completely with the antiferredoxin glutamate synthase immunoglobulin G. In contrast, the immunoglobulin G did not cross-react with NADH-dependent (EC 1.4.1.14) and NADPH-dependent (EC 1.4.1.13) glutamate synthases found in nonphotosynthetic etiolated leaf and root tissues. In addition, ferredoxin-dependent glutamate synthase was separated and distinguished by its affinity to ferredoxin from NAD(P)H-dependent glutamate synthase on ferredoxin-Sepharose affinity chromatography. Based on the immunological studies, it is suggested that ferredoxin-dependent glutamate synthases in green leaf and etiolated leaf tissues are closely related proteins; in contrast, ferredoxin-dependent glutamate synthase in root tissue is a distinct protein from the leaf enzymes.

1 Recipient of a scholarship from the French Foreign Ministry




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Copyright © 1982 by the American Society of Plant Biologists