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. 2000 Jan;11(1):325–337. doi: 10.1091/mbc.11.1.325

Figure 6.

Figure 6

In vitro binding of GST–caveolin-1 fusion proteins to chicken muscle filamin. Samples were separated by SDS-PAGE and electrotransferred onto polyvinylidene difluoride membranes. (Upper panel) A chicken filamin-specific polyclonal antiserum recognizes filamin immunoreactivity of purified chicken muscle filamin (ChF) and in fractions containing GST–caveolin-1-1–101, GST–caveolin-1-1–178, and GST–caveolin-1-32–178. In the control eluate containing GST, only weak, residual binding is detected. (Lower panel) Immunoblot of the GST fusion proteins present in the eluates with the use of an anti-GST mAb. These results extend the data of filamin-28–caveolin-1 binding, showing that full-length caveolin-1 isoforms are able to bind to a muscle filamin isoform. Apparent molecular weights are indicated to the right. f, filamin.