日本語フィールド
著者：Yamashita, Atsushi; Sato, Kazuaki; Watanabe, Masanobu; Tokudome, Yoshihiro; Sugiura, Takayuki; Waku, Keizo題名：Induction of coenzyme A-dependent transacylation activity in rat liver microsomes by administration of clofibrate発表情報：Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism 巻: 1211 号: 3 ページ: 263 - 269キーワード：概要：The effect of administration of clofibrate on the activity of coenzyme A-dependent (CoA-dependent) transacylation of 1-acyl-glycerophosphocholine (1-acyl-GPC) was examined in rat liver microsomes. Administration of clofibrate to rats increased the activity of CoA-dependent transacylation of 1-[14C]acyl-GPC and the activity reached a value (8.37 nmol/min per mg protein) twice that in control rats (3.95 nmol/min per mg protein) without any changes in apparent Km values for CoA (1.2 μM in control and 1.0 μM in clofibrate-treated) and 1-acyl-GPC (33.4 μM in control and 27.8 μM in clofibrate-treated). The rate of CoA-dependent transfer of [14C]arachidonic acid (20:4) from 1-acyl-2-[14C]20:4-glycerophosphoethanolamine (GPE) or 1-acyl-2-[14C]20:4-glycerophosphoinositol (GPI) to 1-acyl-GPC (synthesis of 1-acyl-2-[14C]20:4-GPC) was also increased by treatment with clofibrate (1.9-fold and 1.5-fold increases, respectively). These results suggest that a CoA-dependent transacylation system of 1-acyl-GPC was induced by treatment with clofibrate. © 1994.抄録：英語フィールド
Author：Yamashita, Atsushi; Sato, Kazuaki; Watanabe, Masanobu; Tokudome, Yoshihiro; Sugiura, Takayuki; Waku, KeizoTitle：Induction of coenzyme A-dependent transacylation activity in rat liver microsomes by administration of clofibrateAnnouncement information:Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism Vol: 1211 Issue: 3 Page: 263 - 269An abstract：The effect of administration of clofibrate on the activity of coenzyme A-dependent (CoA-dependent) transacylation of 1-acyl-glycerophosphocholine (1-acyl-GPC) was examined in rat liver microsomes. Administration of clofibrate to rats increased the activity of CoA-dependent transacylation of 1-[14C]acyl-GPC and the activity reached a value (8.37 nmol/min per mg protein) twice that in control rats (3.95 nmol/min per mg protein) without any changes in apparent Km values for CoA (1.2 μM in control and 1.0 μM in clofibrate-treated) and 1-acyl-GPC (33.4 μM in control and 27.8 μM in clofibrate-treated). The rate of CoA-dependent transfer of [14C]arachidonic acid (20:4) from 1-acyl-2-[14C]20:4-glycerophosphoethanolamine (GPE) or 1-acyl-2-[14C]20:4-glycerophosphoinositol (GPI) to 1-acyl-GPC (synthesis of 1-acyl-2-[14C]20:4-GPC) was also increased by treatment with clofibrate (1.9-fold and 1.5-fold increases, respectively). These results suggest that a CoA-dependent transacylation system of 1-acyl-GPC was induced by treatment with clofibrate. © 1994.