Fig. 4

ATP transport into proteoliposomes with the full complement of mammalian ER membrane proteins. Proteoliposomes harboring porcine or canine pancreatic rough ER membrane proteins were prepared as described in Methods. a Time dependent accumulation of 50 µM [α³²P]-ATP in unloaded (pink) or preloaded (10 mM ADP; red) proteoliposomes, which were derived from porcine pancreatic microsomes by treaytment with puromycin and high salt (PKRM). Related substrate saturation experiments and corresponding Eadie–Hofstee analyses are shown in Supplementary Fig. 5. All data are reported as the mean of at least three independent experiments. b Proteoliposomes were preloaded with 10 mM ADP (except for the bar labeled control, which refers to unloaded proteoliposomes). [α³²P]-ATP was present at a concentration of 50 µM. Each effector substance was given at a concentration of 500 µM and uptake was terminated after 2 min. All data are reported as the mean of at least three independent experiments and are shown with the standard error of the mean (SEM)