Fig. 2.
Fig. 2. Binding of ABC7 to ferrochelatase. / (A) Effect of deletions in GST-ABC7 on binding to ferrochelatase. GST, GST-ABC7 (458-752), GST-ABC7 (521-752), and GST-ABC7 (596-752) were immobilized on glutathione beads, after which they were incubated with partially purified ferrochelatase. Bound proteins were analyzed by SDS-PAGE, followed by immunoblotting with antiferrochelatase. Input: A Coomassie blue staining of GST-ABC7 fusion proteins bound to glutathione beads. (B) Effect of deletion of ferrochelatase (FECH) on binding to GST-ABC7 (458-752). Partially purified ferrochelatase (wild-type) and a mutant (N395Δ) expressed in E coli were incubated with GST-ABC7 (458-752) immobilized on the beads. Bound proteins were analyzed by SDS-PAGE, followed by immunoblotting with antiferrochelatase. Input: Coomassie blue staining of partially purified ferrochelatase.

Binding of ABC7 to ferrochelatase.

(A) Effect of deletions in GST-ABC7 on binding to ferrochelatase. GST, GST-ABC7 (458-752), GST-ABC7 (521-752), and GST-ABC7 (596-752) were immobilized on glutathione beads, after which they were incubated with partially purified ferrochelatase. Bound proteins were analyzed by SDS-PAGE, followed by immunoblotting with antiferrochelatase. Input: A Coomassie blue staining of GST-ABC7 fusion proteins bound to glutathione beads. (B) Effect of deletion of ferrochelatase (FECH) on binding to GST-ABC7 (458-752). Partially purified ferrochelatase (wild-type) and a mutant (N395Δ) expressed in E coli were incubated with GST-ABC7 (458-752) immobilized on the beads. Bound proteins were analyzed by SDS-PAGE, followed by immunoblotting with antiferrochelatase. Input: Coomassie blue staining of partially purified ferrochelatase.

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