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. 1997 Nov 3;139(3):589–599. doi: 10.1083/jcb.139.3.589

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Extent of ER membrane targeting of P4501A1 under in vitro conditions. (A) P4501A1, P450 reductase, and DHFR were cotranslated in rabbit reticulocyte lysate in the presence or absence of unwashed canine pancreatic ER. The reaction mixtures were extracted with 0.1 M Na₂CO₃, pH 11.5, and the alkaline-soluble and -insoluble fractions were recovered and concentrated as described recently (Anandatheerthavarada et al., 1997). Protein fractions equivalent of 5 μl of initial reaction mixture in each case were subjected to electrophoresis and autoradiography. (B) The gel patterns for the alkaline-soluble and -insoluble fractions in A were quantitated in a PhosphorImager to determine the percentage of recovery in the membrane integral (Membrane Fraction) and extrinsic (Aqueous Fraction) fractions, respectively. Values represent the average of two experiments.

Extent of ER membrane targeting of P4501A1 under in vitro conditions. (A) P4501A1, P450 reductase, and DHFR were cotranslated in rabbit reticulocyte lysate in the presence or absence of unwashed canine pancreatic ER. The reaction mixtures were extracted with 0.1 M Na₂CO₃, pH 11.5, and the alkaline-soluble and -insoluble fractions were recovered and concentrated as described recently (Anandatheerthavarada et al., 1997). Protein fractions equivalent of 5 μl of initial reaction mixture in each case were subjected to electrophoresis and autoradiography. (B) The gel patterns for the alkaline-soluble and -insoluble fractions in A were quantitated in a PhosphorImager to determine the percentage of recovery in the membrane integral (Membrane Fraction) and extrinsic (Aqueous Fraction) fractions, respectively. Values represent the average of two experiments.