Partial purification and characterization of fatty acid binding protein(s) in Escherichia coli membranes and reconstitution of fatty acid transport system.
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.
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
D002352:Carrier Proteins; D050556:Fatty Acid-Binding Proteins; D005227:Fatty Acids; D008081:Liposomes; D009363:Neoplasm Proteins