Call F L, Rubert M
J Lipid Res. 1975 Sep;16(5):352-9.
Platelet homogenates contain an ethanolaminephosphotransferase (EC 2.7.8.1) that catalyzes the synthesis of ethanolamine phosphoglycerides from cytidine-5'-diphosphate ethanolamine and 1-radyl-2-acyl-sn-glycerols. The enzyme is particulate-bound and requires Mn2+ and bile salts for optimal activity. The apparent Km of the enzyme for cytidine-5'-diphosphate ethanolamine is 1.6 X 10(-5) M when the concentration of 1,2-diacyl-sn-glycerols is 8.8 X 10(-4) M. The pH optimum is 8.5 in Tris-HCl or glycine-NaOH buffer. The activity of the enzyme in platelets from normal subjects is 0.24-0.34 nmole/min/mg of protein.
血小板匀浆含有一种乙醇胺磷酸转移酶（EC 2.7.8.1），它催化由胞苷-5'-二磷酸乙醇胺和1-酰基-2-酰基-sn-甘油合成乙醇胺磷酸甘油酯。该酶与颗粒结合，需要Mn2+和胆盐以达到最佳活性。当1,2-二酰基-sn-甘油的浓度为8.8×10(-4) M时，该酶对胞苷-5'-二磷酸乙醇胺的表观Km为1.6×10(-5) M。在Tris-HCl或甘氨酸-NaOH缓冲液中，最适pH为8.5。正常受试者血小板中该酶的活性为0.24 - 0.34纳摩尔/分钟/毫克蛋白质。
