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Plant Physiology 66:619-623 (1980)
© 1980 American Society of Plant Biologists

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Articles

Glutamine Synthetase in Rice

A COMPARATIVE STUDY OF THE ENZYMES FROM ROOTS AND LEAVES 1

Bertrand Hirel and Pierre Gadal

Laboratoire de Biologie Végétale, Era No. 799, Université de Nancy I, 54037 Nancy Cedex, France

Chromatographic, kinetic, and regulatory properties of glutamine synthetase in rice were investigated. By DEAE-Sephacel column chromatography, two forms (glutamine synthetase 1 and glutamine synthetase 2) were identified in leaves and one form (glutamine synthetase R) was identified in roots. Purification on hydroxyapatite and gel electrophoresis showed that glutamine synthetase R was distinct from the leaf enzymes. The three isoforms were purified to similar specific activities and their properties were studied. Heat lability, pH optimum about 8, Km for L-glutamate of 20 millimolar, and inhibition by glucosamine 6-phosphate were the main characteristics of glutamine synthetase 2. Heat stability, pH optimum about 7.5, Km for L-glutamate of 2 millimolar, and no effect of glucosamine 6-phosphate differentiated glutamine synthetase 1 from glutamine synthetase 2. Glutamine synthetase R was also a labile protein but its kinetic and regulatory properties were quite similar to those of glutamine synthetase 1. These results clearly demonstrate the existence of three isoforms of glutamine synthetase in rice, two of which are located in the leaves and the third in the roots.

1 This work was supported by Grant RCP 389 from the Centre Nationale de la Recherche Scientifique and by Grant No. 78 70 445 from the Direction Générale à la Recherche Scientifique et Technique.




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