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. 2004 Feb;78(3):1367–1374. doi: 10.1128/JVI.78.3.1367-1374.2004

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Copyright © 2004, American Society for Microbiology

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FIG. 2. — Data used for calculating the average number of copies of pU_L15 or pU_L28 in capsids. (A) Coomassie-stained gel with B capsids (lanes 1 and 2) and BSA standards (lanes 3 to 8). The amount of BSA (in nanograms) loaded is indicated at the bottom of lanes 3 to 8. The R² value of the graph produced by analysis of the data was 0.98, and the estimated amount of VP5 (arrow) is indicated in italics below lanes 1 and 2. The positions of molecular weight standards are indicated on the left. (B) Immunoblot of B capsids (lanes 1 and 2) and purified U_L15 protein standards (lanes 3 to 8) probed with antisera directed against pU_L15. The amount of pU_L15 (in nanograms) is indicated below each lane. (C) Immunoblot probed with antisera directed against pU_L28. B capsids are in lanes 1 and 2, and purified U_L28 protein standards are in lanes 3 to 9. The amount of pU_L28 (in nanograms) is indicated below each lane.

FIG. 2. — Data used for calculating the average number of copies of pU_L15 or pU_L28 in capsids. (A) Coomassie-stained gel with B capsids (lanes 1 and 2) and BSA standards (lanes 3 to 8). The amount of BSA (in nanograms) loaded is indicated at the bottom of lanes 3 to 8. The R² value of the graph produced by analysis of the data was 0.98, and the estimated amount of VP5 (arrow) is indicated in italics below lanes 1 and 2. The positions of molecular weight standards are indicated on the left. (B) Immunoblot of B capsids (lanes 1 and 2) and purified U_L15 protein standards (lanes 3 to 8) probed with antisera directed against pU_L15. The amount of pU_L15 (in nanograms) is indicated below each lane. (C) Immunoblot probed with antisera directed against pU_L28. B capsids are in lanes 1 and 2, and purified U_L28 protein standards are in lanes 3 to 9. The amount of pU_L28 (in nanograms) is indicated below each lane.