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Figure 1 | BMC Biochemistry

Figure 1

From: p42MAPK-mediated phosphorylation of xEIAP/XLX in Xenopus cytostatic factor-arrested egg extracts

Figure 1

Phosphorylation-dependent electrophoretic mobility shift of xEIAP/XLX in CSF-arrested egg extracts. (A) Schematic models of recombinant proteins used in this study. (B) Time-dependent changes of recombinant proteins incubated in CSF-arrested (CSF) and interphase (INT) egg extracts. 35S-radiolabeled 6XHis-FL, MBP-FL, MBP-Δ1, and MBP-Δ2 were mixed with either CSF-arrested or interphase egg extracts and incubated for indicated time periods (0, 2, and 4 h). After separation by SDS-PAGE, radiolabeled and MBP-fused recombinants were detected by image analyzer and Western blot, respectively. Molecular weights of standard proteins are indicated at the left. The larger (~70 k) and smaller cleavage products (50–55 k) of MBP-fusions are indicated by single and double asterisks, respectively. (C) Phosphorylation-dependent electrophoretic mobility shift of xEIAP/XLX. Endogenous xEIAP/XLX in CSF-arrested egg extracts were retrieved by antibody-coated beads and incubated with (+) or without (-) calf intestine alkaline phosphatase. After separation by SDS-PAGE, xEIAP/XLX was detected by Western blot. Positions of phosphorylated (P-xEIAP) and unphosphorylated (xEIAP) forms of xEIAP/XLX are indicated by arrowheads. The position of IgG heavy chain (IgG HC) is indicated by the line.

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