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作者机构:Department of Biological Chemistry The University of Michigan Ann Arbor Michigan 48104
出 版 物:《Journal of Biological Chemistry》 (J Biol Chem)
年 卷 期:1968年第243卷第10期
页 面:2654-2659页
学科分类:0710[理学-生物学] 0831[工学-生物医学工程(可授工学、理学、医学学位)] 071010[理学-生物化学与分子生物学] 07[理学] 0703[理学-化学]
摘 要:Acylation of 1- O -(1′-alk-1′-enyl)-glycero-3-phosphorylcholine by long chain acyl thiol esters of coenzyme A to form plasmalogens was catalyzed by enzymes from erythrocytes and muscle. The alkenyl acyl phosphoglycerides produced were the type of plasmalogen most commonly present in mammalian tissues. Enzymes catalyzing this reaction are located in membrane fractions that also contain acyl transfer activity for other phospholipids. Acyl transfer rates with oleoyl-, linoleoyl-, and arachidonoyl-CoA were 13, 27, and 27 mµmoles per min per mg of protein, respectively, with the acyl analogue that forms lecithin, whereas they were 1, 9.4, and 4.7, respectively, with the alkenyl derivative that forms plasmalogen.