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. 2011 Feb 25;286(15):13346–13356. doi: 10.1074/jbc.M110.216416

FIGURE 2.

FIGURE 2.

Specific detergents maintain TAP function. A, solubilization efficiency in different detergents. Crude membranes (500 μg of protein) were solubilized in different detergents (2%, w/v). Detergent extracts were analyzed by SDS-PAGE (10%) and immunoblotting. The solubilization efficiency of TAP1 (black bars) and TAP2 (gray bars) was compared with the total amount of TAP in crude membranes (cm). UDM, n-undecyl-β-d-maltoside; FC-14, Fos-Choline-14; OG, n-octylglucoside; TX-100, Triton X-100; NP40, Nonidet P-40; LDAO, lauryldimethylamine-oxide. B, TAP function in different detergents. Crude membranes were solubilized (as described in A), and peptide binding of solubilized TAP was probed with 125I-labeled peptide RRYQKSTEL (1 μm) in the presence or absence of 200-fold excess of unlabeled peptide. Specific binding was normalized to that observed in digitonin, which gave the highest binding efficiency. Each data point represents the mean of triplicate measurements; error bars show S.D. Asterisk: no binding detectable. C, long-term stability of solubilized TAP. Peptide binding to TAP was analyzed after several days of incubation at 4 °C and normalized to specific binding at day 1 in the presence of digitonin. Error bars show S.D.