Tai S P, Kaplan S
J Biol Chem. 1984 Oct 10;259(19):12178-83.
A phospholipid transfer protein has been purified 280-fold from Rhodopseudomonas sphaeroides when compared to the 40-70% ammonium sulfate fraction derived from the crude cell supernatant in which the activity was originally found (Cohen, L.K., Lueking, D.R., and Kaplan, S. (1979) J. Biol. Chem. 254, 721-728). When compared to the crude cell lysate, the activity has been purified approximately 1,400-fold with a recovery of 12.5%. The active protein is a monomer with a molecular weight of 26,500, as estimated by sedimentation velocity and sedimentation equilibrium, and 27,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The protein can transfer all phospholipid species tested with the order of efficiency of transfer being phosphatidylglycerol greater than phosphatidylcholine greater than phosphatidylethanolamine.
与最初发现活性的粗细胞上清液中40%-70%硫酸铵分级分离物相比，从球形红假单胞菌中纯化出一种磷脂转移蛋白，纯化了280倍（科恩，L.K.，卢金，D.R.，和卡普兰，S.（1979年）《生物化学杂志》254，721-728）。与粗细胞裂解物相比，该活性已纯化约1400倍，回收率为12.5%。通过沉降速度和沉降平衡估计，活性蛋白是一种分子量为26500的单体，通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳估计为27000。该蛋白可以转移所有测试的磷脂种类，转移效率顺序为磷脂酰甘油大于磷脂酰胆碱大于磷脂酰乙醇胺。
