@article{oai:swu.repo.nii.ac.jp:00002367,
 author = {松本, 孝 and Matsumoto, Takashi},
 journal = {昭和女子大学大学院生活機構研究科紀要, Bulletin of the Graduate School of Human Life Sciences, Showa Women's University},
 month = {Mar},
 note = {An obligate methylotrophic bacterium, Methylomonas sp. J is able to grow on only two C-1 compounds, methanol and methylamine. In our previous study (2), it was suggested that the glutamine synthetase was a preferred enzyme as the nitrogen assimilation in the cells, when nitrate and methanol were the respective nitrogen and carbon sources for this micro-organism. While, when methylamine was only nitrogen and carbon source, it was shown that two enzyme activities, glutamine synthetase and NADP-depenndent glutamate dehydrogenase activities were detected. From these observations, much interest has focused on the regulation of the glutamine synthetase activity in assimilation of nitrogen. The aim of this study was to characterize glutamine synthetase from Methylomonas sp. J in different nitrogen sources. so, at first, glutamine synthetase of this micro-organism was purified to homogeneity from the cells grown in synthetic medium of methanol and nitrate as carbon and nitrogen sources, respectively. The purified enzyme had a molecular weight of 580,000 and a subunit size of 55,000. The studies of the effect on the catalytic properties by snake venom phosphodiesterase treatment suggest this enzyme is regulated by adenylation/deadenylation. The release of AMP from the enzyme was also detected by the treatment. Some other properties of the enzyme, such as Km for each substrate, inhibition by some metabolites and effect of metal-ions were determined and compared to those in the case of other bacterial enzymes., 7, KJ00004311150},
 pages = {55--64},
 title = {偏性C 1化合物資化性菌Methylomonas sp. Jが生産するglutamine synthetaseの精製と性質},
 volume = {8},
 year = {1999},
 yomi = {マツモト, タカシ}
}