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. 2001 Oct;75(19):8968–8976. doi: 10.1128/JVI.75.19.8968-8976.2001

FIG. 4.

FIG. 4

Electrophoretic mobility shift assays for the AAV D(−) sequence (lane 1) interaction with human FKBP52 purified from bacterial cells without (lane 2) and with prior in vitro phosphorylation with CK II (lane 3) and EGFR-PTK (lane 5), respectively. These assays were performed as described in Materials and Methods. No interaction between the probe and CK II alone (lane 4) or EGFR-PTK alone (lane 6) was observed. Complexes presumed to contain the phosphorylated forms of the FKBP52 protein are denoted by the solid arrows and arrowhead, and the unphosphorylated form is denoted by the open arrowhead.