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Fig. 2 | BMC Molecular and Cell Biology

Fig. 2

From: Characterization and engineering of a DNA polymerase reveals a single amino-acid substitution in the fingers subdomain to increase strand-displacement activity of A-family prokaryotic DNA polymerases

Fig. 2

Temperature stability of polymerase I large fragment from Psychrobacillus sp. The thermal stability has been measured using the single-nucleotide incorporation endpoint assay and densitometric analysis (line chart at the bottom) of the bands after denaturing polyacrylamide gel electrophoresis (12% polyacrylamide/7 M urea, gel on top, neg. = negative control). After incubation of the reaction set-ups at the respective temperature the enzymatic reaction has been performed in 50 mM BIS-Tris propane pH 8.5 (at 25 °C), 100 mM NaCl, 5 mM MgCl2, 1 mM DTT, 0.2 mg/ml BSA and 2% glycerol. For the reactions 180 pg protein were used

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BMC Molecular and Cell Biology

ISSN: 2661-8850

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