Fig. 8.
Fig. 8. Competitive binding of α18-21, α18-211857, or α18-211857-Δ46 to GSTβ1-4+. In each assay, 250 pmol of 35S α18-21 and 250 pmol of GSTβ1-4+ were mixed with 0, 125, 250, 500, and 1,000 pmol of each competitor (α18-21, α18-211857, or α18-211857-Δ46) in a final volume of 400 μL in PBS/0.1% bovine serum albumin for 30 minutes on ice. Bound complexes were sedimented with glutathione Sepharose 4B in a Millipore 0.22-μm filtration unit and the filtrate was counted as the unbound fraction. The resin was washed twice and bound complexes were eluted with two aliqouts of 400 μL 0.2% SDS. Background corrected values for the amount of 35S α18-21 from three different experiments were averaged (error bars show standard deviation). () α18-21; () α18-211857; (▪) α18-211857-Δ46.

Competitive binding of α18-21, α18-211857, or α18-211857-Δ46 to GSTβ1-4+. In each assay, 250 pmol of 35S α18-21 and 250 pmol of GSTβ1-4+ were mixed with 0, 125, 250, 500, and 1,000 pmol of each competitor (α18-21, α18-211857, or α18-211857-Δ46) in a final volume of 400 μL in PBS/0.1% bovine serum albumin for 30 minutes on ice. Bound complexes were sedimented with glutathione Sepharose 4B in a Millipore 0.22-μm filtration unit and the filtrate was counted as the unbound fraction. The resin was washed twice and bound complexes were eluted with two aliqouts of 400 μL 0.2% SDS. Background corrected values for the amount of 35S α18-21 from three different experiments were averaged (error bars show standard deviation). () α18-21; () α18-211857; (▪) α18-211857-Δ46.

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