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Purification and properties of a cytosolic glutamine synthetase expressed in Nicotiana plumbaginifolia cultured cells.



Glutamine synthetase (EC was purified and characterized from leaf protoplast-derived suspension cultured cells of Nicotiana plumbaginifolia. Maximal specific activity observed reflected a purification of over 1 500-fold, with a yield of about 40%. The native protein appeared to be an octamer, with subunits of a molecular mass of 37 kDa. Subcellular fractionation experiments accounted for a cytosolic localization of the enzyme. No evidence for multiple enzyme forms was found following either anion-exchange chromatography or native polyacrylamide gel electrophoresis. Results also suggest that in the absence of intercellular transport, type-1 glutamine synthetase may function preferentially to assimilate ammonia from primary nitrate reduction

Topics: ammonia assimilation, cultured cells, glutamine synthetase isoenzymes, Nicotiana plumbaginifolia, subunit composition
Year: 2000
DOI identifier: 10.1016/S0981-9428(00)00732-4
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