Summary
Glutamine synthetase I was purified fromRhizobium sp. UMKL 20 following polyethylene glycol precipitation. The enzyme had a subunit molecular weight of 58 kd. Apparent Km values for ammonia and glutamate were 5.6 and 15.2 mM, respectively. Glutamine synthetase I activity was inhibited by several end products of glutamine metabolism. The purified enzyme was highly adenylylated (E −n =8.5).
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Acknowledgment. I would like to thank Mr J. C. Lai for technical assistance. This work was carried out with the support of Vote F 153/79 from the University of Malaya.
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Lim, S.T. Purification and properties of glutamine synthetase I fromRhizobium sp. UMKL 20. Experientia 41, 727–728 (1985). https://doi.org/10.1007/BF02012567
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DOI: https://doi.org/10.1007/BF02012567