Purification and properties of a phospholipid transfer protein from Rhodopseudomonas sphaeroides.
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.
D002352:Carrier Proteins / Q000302:isolation & purification*; D002499:Centrifugation, Density Gradient; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D007526:Isoelectric Point; D008565:Membrane Proteins; D008970:Molecular Weight; D049294:Phospholipid Transfer Proteins; D010743:Phospholipids / Q000378:metabolism*; D012242:Rhodobacter sphaeroides / Q000032:analysis*; D013997:Time Factors
D002352:Carrier Proteins; D008565:Membrane Proteins; D049294:Phospholipid Transfer Proteins; D010743:Phospholipids