Purification and properties of glutamine synthetase I fromRhizobium sp. UMKL 20 |
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| Authors: | S. T. Lim |
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| Affiliation: | (1) Department of Biochemistry, University of Malaya, Lembah Pantai, Kuala Lumpur, Malaysia |
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| Abstract: | 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 (En–=8.5).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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| Keywords: | Rhizobium glutamine synthetase I |
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