Monoamine Oxidaseに関する研究-9-精製MAOに対する燐脂質ならびに金属イオンの影響

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Monoamine Oxidase (MAO) in hog kidney was partially purified and the enzymic properties of the purified MAO were studied. The effect of metal-ions and phospholipid on the purified MAO were studied and the following results were obtained ;<BR>1) MAO in mitochondria was solublized by the treatment of 1 % sodium cholate and purified by the ammonium sulfate fractionation. The specific activity of the purified MAO was about 13-folds than that of homogenate.<BR>2) In case of phosphate buffer used as medium, MAO activities were found both in 10 to 20% and 30 to 40 % saturated fraction, while in case of Tris buffer (used as medium), they were found in 10 to 20% and 50 to 60% saturated fraction.<BR>3) The effect of metal-ions on MAO activity was studied comparing with the case of the homogenate and the purified MAO. Ca _??_, Co _??_, Ba _??_ and Pb _??_ caused less inhibition of the activity of the purified MAO than that of the homogenate. However, Fe _??_, Cu _??_, Cd _??_ and Hg _??_ caused markedly inhibi-tion to the activity of the purified MAO.<BR>4) Lecithin caused activation of the purified MAO. Especially 1 % Lecithin caused increase of MAO activity about 2-3 folds than that of the control.
学校法人昭和大学・昭和医学会の論文