モルモット肝ミクロソームのカルボニル還元酵素活性と膜脂質との相互作用

概要

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Membrane lipids affecting guinea pig liver microsomal carbonyl reductase were investigated. The reductase in microsomes treated with 67% acetone was activated about three times that of intact microsomes, and inhibited by the addition of acetone-extracted lipids. The fatty acids, such as palmitic acid, stearic acid and oleic acid which were detected in acetone-extracted lipids, strongly inhibited the reductase in acetone-treated microsomes and the purified reductase, and the K_i value of palmitic acid for the purified reductase was 50 μM. These fatty acids may be able to regulate the reductase activity physiologically. On the other hand, the activity of reductase was inactivated by phospholipase treatment and delipidation of microsomes with sodium deoxycholate, and recovered by the addition of phospholipids (e. g. lysophosphatidylcholine, sphingomyelin and phosphatidylcholine) in phospholipase-treated and delipidated microsomes. The purified reductase was reactivated by phospholipids such as lysophosphatidylcholine, phosphatidylserine and phosphatidylcholine. Triton X-100 also gave a similar effect to phospholipid, and was able to be substituted for phospholipid in supporting the reducatse activity. These results indicate that the membrane lipids take part in carbonyl reductase activity.
公益社団法人日本薬学会の論文
1985-03-25