@article{oai:u-ryukyu.repo.nii.ac.jp:02003082,
 author = {安田, 正昭 and 当山, 清善 and 与那覇, 和雄 and 左右田, 健次 and Yasuda, Masaaki and Toyama, Seizen and Yonaha, Kazuo and Soda, Kenji},
 issue = {28},
 journal = {琉球大学農学部学術報告, The Science Bulletin of the Faculty of Agriculture. University of the Ryukyus},
 month = {Nov},
 note = {Corynebacterium sepedonicum(IFO 3306)の無細胞抽出液中にL-オルニチンをアミノ基供与体としたアミノ基転移反応を触媒するトランスアミナーゼの存在が明らかになった。最も高い酵素活性は, 本菌株をL-オルニチン(0.3%)またはL-アルギニンを添加した培地(ペプトン, グリセリンを含む)でpH7.2,30℃, 18-20時間振とう培養して得た菌体で得られた。本酵素は培地中のL-オルニチンまたはL-アルギニンにより誘導的に生成された。本酵素はL-オルニチンとα-ケトグルタル酸との間のアミノ基転移反応を触媒しL-グルタミン酸を生成し, 化学量論的に反応が進行した。本酵素の反応最適pHは8.0で, 反応最適温度は45℃であった。, The production and some properties of the enzyme which catalyzes transamination between L-ornithine and α-ketoglutarate were described. The enzyme was found in the cell-free extract of Corynebacterium sepedonicum (IFO 3306). In order to find the medium conditions required for the improvement of the enzyme production by this strain, the organism was grown in the medium contaning L-ornithine or L-arginine. The best enzyme production was obtained when the organism was grown in the medium (initial pH 7.2) contaning L-ornithine (0.3%) at 30℃ for 18-20hr under aerobic conditions. The cell-free extract of the strain grown under the conditions mentioned above catalyzed the transamination reaction between L-ornithine and α-ketoglutarate to produce L-glutamate. This enzymatic transamination was found to proceed stoichiometrically. The enzyme had the maximum reactivity at pH 8.0 and 45℃ for the transamination reaction., 紀要論文},
 pages = {101--109},
 title = {Corynebacterium sepedonicum の L-オルニチントランスアミナーゼ(農芸化学科)},
 year = {1981}
}