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• W2038331410 abstract "A relatively rapid five-step procedure was used in purifying to apparent homogeneity the glutamine synthetase from roots and one form of the enzyme (GSI) from leaves of rice. The steps were: preparation of crude extracts, ammonium sulfate precipitation, filtration on Sepharose 4B, fractionation on DEAE-Sephadex A25, and affinity chromatography on ADP-Sepharose 4B. The purified protein appeared as a single band on polyacrylamide gel electrophoresis. Leaf GSI and the second type of leaf glutamine synthetase (GSII) formed distinct peaks when eluted from DEAE-Sephadex (step 4). The root enzyme and leaf GSI were similar in all the properties which were examined. Both enzymes bound to ADP-Sepharose, had similar biosynthetic (18 μmol P/img protein/min) and transferase (1324 and 1156 μmol γ-glutamyl hydroxamate/mg protein/min) activities, and the same or nearly the same Km values for glutamate (2.17 mm), Mg2+ (4.5 and 5.0 mm), ATP (286 μm), NH4+ (210 and 135 μm), and ADP (3.8 and 5.3 μm). In contrast, leaf GSII did not bind to ADP-Sepharose and had much higher Km values for glutamate (8.3 mm), Mg2+ (15 mm), NH4+ (684 μm), and ADP (33 μm)." @default.
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• W2038331410 date "1981-07-01" @default.
• W2038331410 modified "2023-09-26" @default.
• W2038331410 title "Glutamine synthetases from rice: Purification and preliminary characterization of two forms in leaves and one form in roots" @default.
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• W2038331410 doi "https://doi.org/10.1016/0003-9861(81)90322-2" @default.
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