@article{oai:fukuyama-u.repo.nii.ac.jp:00007431,
 author = {吉田, 美夫 and 沖増, 英治 and 雨村, 明倫},
 journal = {福山大学附属内海生物資源研究所報告},
 month = {Dec},
 note = {P(論文), ニジマス白血球の15-LO酵素の分子量は約70,000であり,哺乳類の15-LO酵素の分子量とも類似していた。至適反応pHは7.5であり,これも至適反応pH7.0をもつ哺乳類と類似していた。しかし,至適反応温度は15℃であり,これは至適反応温度を高温領域にもつ哺乳類とは異なっていた。ニジマス白血球の15-LO酵素の最終精製段階における回収率は3.1%,精製純度が4.8倍と非常に不安定な酵素であることが明らかになった。, 15-Lipoxygenase activity with arachidonic acid as a substrate was detected in leukocyte extract from the kidney of rainbow trout (Oncorhynchus mykiss). 15-Lipoxygenase was purified by gel filtration followed by hydroxyapatite chromatography. The enzyme activity towards arachdonic acid was highest at pH 7.5 and at temperatures between 10℃ and 20℃. The molecular weight of enzyme estimated by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate (SDS-PAGE) was 70,000 near that of the enzyme from human leukocyte (65,000-75,000)[E.Sigal et.al : J. Biol. Chem., 263, 5328-5332(1988)].},
 pages = {1--12},
 title = {ニジマス白血球のアラキドン酸15-リポキシゲナーゼの精製とその諸性質},
 volume = {4},
 year = {1993}
}