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. 2001 Sep;21(17):5913–5924. doi: 10.1128/MCB.21.17.5913-5924.2001

FIG. 4.

FIG. 4

N terminus of AMF1 interacts with p53. Six-histidine-tagged wild-type and mutant AMF1 proteins were prepared by in vitro translation. These proteins (named by the number of amino acids contained) were incubated with Sf9 cell extract containing either papillomavirus E1 (lanes 2, 5, 8, and 11) or p53 (lanes 3, 6, 9, and 12), in the presence of MAb pAb421 against p53. Immunocomplexes were precipitated with protein A-Sepharose. After washing, AMF1 proteins remaining on the beads were run on an SDS–15% polyacrylamide gel together with 10% volume of each input (lanes 1, 4, 7, 10). The gel was analyzed with a Bio-Rad GS-250 molecular imager.