@article{oai:u-ryukyu.repo.nii.ac.jp:02003118,
 author = {石原, 昌信 and 与那覇, 和雄 and 当山, 清善 and Ishihara, Masanobu and Yonaha, Kazuo and Toyama, Seizen},
 issue = {27},
 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 = {各種カビにおけるL-アラニン : α-ケトグルタル酸トランスアミナーゼ活性を調べた結果, 泡盛麹菌(Asp. awamori IFO4122)を蔗糖-ペプトン含有培地で振とう培養し, 得られた菌体の無細胞抽出液中に高い酵素活性が得られた。本酵素はL-アラニンとα-ケトグルタル酸からL-グルタミン酸とピルビン酸を生成するアミノ基転移反応を触媒し, 本反応の逆反応も触媒した。本酵素は, 供試泡盛麹菌株の無細胞抽出液から硫安分画及び各種のカラムクロマトグラフィーにより55倍に精製された。精製酵素のゲル滬過法で求めた分子量は104,000であり, 吸収スペクトルは280nm, 320nm及び418nmに吸収極大があった, 精製酵素はL-アラニンに特異的で, L-アラニン及びα-ケトグルタル酸に対するkm値は2.9mMであった。酵素反応の至適pHは7.0∿8.0で, 至適温度は45℃であった。, The activity of L-alanine : α-ketoglutarate transaminase in the cell-free extracts of various molds has been determined. A high activity of the transaminase was found in the cell-free extract of Aspergillus awamori IFO 4122 grown on sucrose-peptone medium with shaking, and the strain was chosen for characterization and purification of the enzyme. The enzyme catalyzed reversibly the transamination between L-alanine and α-ketoglutarate producing L-glutamate and pyruvate. The enzyme was purified 55 fold from the cell-free extract, using ammonium sulfate fractionation and various chromatographic techniques. A molecular weight of 104,000 was obtained by gel filtration. The purified enzyme exhibits absorption maxima at 280nm, 320nm and 418nm, at pH 8.0. The purified enzyme was highly specific for L-alanine and the Km value for L-alanine and α-ketoglutarate was estimated to be 2.9mM. The optimal pH and temperature for the transaminase reaction were 7.0-8.0 and 45℃, respectively., 紀要論文},
 pages = {89--102},
 title = {泡盛麹菌の L-アラニン : α-ケトグルタル酸トランスアミナーゼの精製と性質(農芸化学科)},
 year = {1980}
}