Fluorescence anisotropy of a fatty acid covalently linked in vivo to the glycoprotein of vesicular stomatitis virus.
The covalently-attached fatty acid of the membrane glycoprotein (G) of vesicular stomatitis virus was fluorescently labeled biologically by isolating vesicular stomatitis virus from infected baby hamster kidney clone 21 cells that had been grown in the presence of 16(9-anthroyloxy)palmitate. The fluorescent labeling was specific for the G protein; the other viral membrane protein, the matrix (M) protein, was not labeled. Steady state fluorescence anisotropy of the 16(9-anthroyloxy)palmitate-labeled G protein reconstituted into dipalmitoylphosphatidylcholine vesicles indicated that the fatty acid attached to G protein is located in a dipalmitoylphosphatidylcholine domain that does not undergo the gel to liquid-crystalline phase transition.
D000818:Animals; D002460:Cell Line; D006224:Cricetinae; D005227:Fatty Acids / Q000032:analysis*; D005454:Fluorescence Polarization; D006023:Glycoproteins / Q000032:analysis*; D007668:Kidney; D007700:Kinetics; D013696:Temperature; D014721:Vesicular stomatitis Indiana virus / Q000032:analysis*; D014764:Viral Proteins / Q000032:analysis*
D005227:Fatty Acids; D006023:Glycoproteins; D014764:Viral Proteins