title: Partial purification and characterization of fatty acid binding protein(s) in Escherichia coli membranes and reconstitution of fatty acid transport system.
abstract: Fatty acid binding protein(s) in E. coli membranes was solubilized and partially purified by oleate-AH Sepharose 4B column chromatography. The binding of palmitate to the protein was saturable. The protein bound all fatty acids with chain lengths of 10-18 tested, and its maximum activity was observed with palmitate. The incorporation of the protein into liposomes which contained a system for acyl-CoA synthesis significantly increased the uptake of the extracellular [14C] palmitate by the liposomes in comparison with the liposomes without the protein. The uptake of [14C] palmitate was also saturable, and the accumulated radioactive compound was found to be palmitoyl-CoA.
mesh_terms: D001692:Biological Transport; D002352:Carrier Proteins / Q000302:isolation & purification* / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism; D002846:Chromatography, Affinity; D004926:Escherichia coli / Q000378:metabolism*; D050556:Fatty Acid-Binding Proteins; D005227:Fatty Acids / Q000378:metabolism*; D007700:Kinetics; D008081:Liposomes; D009363:Neoplasm Proteins
chemical_list: D002352:Carrier Proteins; D050556:Fatty Acid-Binding Proteins; D005227:Fatty Acids; D008081:Liposomes; D009363:Neoplasm Proteins