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The reaction mixtures were resolved by a native polyacrylamide gel followed by autoradiography.
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Native PAGE: The traditional Tris glycine system was used; the proteins were separated by using a native polyacrylamide gel (12%%).
PCL-degrading activity was detected by zymography by separating the proteins in a native polyacrylamide gel.
The catalase activity was also visualized by catalase activity staining on a native polyacrylamide gel.
Briefly, protein extracts (6 μg) were incubated for 30 min at room temperature with radiolabeled DNA probes containing a consensus kB site, separated on a native polyacrylamide gel, and visualised by autoradiography.
The resulting DNA was amplified by PCR using primers A and B, and amplified DNA was electrophoresed on a native polyacrylamide gel (BioRad).
A native polyacrylamide gel electrophoresis (native-PAGE) was prepared as previously described [ 15].
The annealed duplex was purified by a 15% native polyacrylamide gel electrophoresis in TBE buffer (45 mmol/L Tris, 45 mmol/L boric acid, 2 mmol/L EDTA, pH 8.0) and dissolved in TE buffer to yield a 10 nmol/L substrate.
The proteins were separated by electrophoresis on a 10% native polyacrylamide gel according to the procedures described by Davis et al [20] in the absence of SDS and 2-mercaptoethanol.
SA-DNA complexes were separated from free DNA by electrophoresis on a 6% native polyacrylamide gel in Tris-taurine buffer (90 mM Tris, 30 mM taurine, pH 7.5).
The DNA-protein complexes were separated by electrophoresis on a 6% native polyacrylamide gel for 1.5 to 2.5 h at 4 °C and 100 V, and the complexes were visualized by autoradiography.
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