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Fig. 1 | BMC Molecular and Cell Biology

Fig. 1

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. 1

A-D Basic characterization of polymerase I large fragment from Psychrobacillus sp. The effect of pH (a), salt (b) and Mg2+ (c, inset showing polymerase activity at 0–40 mM MgCl2) have been measured with the time-resolved molecular beacon assay at 25 °C. The increase in Fluorescein fluorescence, i.e. enzyme activity, has been measured as relative fluorescence units (RFUs). For the reactions 37.5 ng protein were used. Effect of temperature (d) on the polymerase activity was tested with the single-nucleotide incorporation endpoint assay and densitometric analysis of the bands after denaturing polyacrylamide gel electrophoresis (12% polyacrylamide/7 M urea). For the reactions 180 pg protein were used. The gel is shown on top (neg. = negative control) and the evaluation of the densitometry at the bottom

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BMC Molecular and Cell Biology

ISSN: 2661-8850

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