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. 2012 Nov 11;41(1):405–417. doi: 10.1093/nar/gks1000

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© The Author(s) 2012. Published by Oxford University Press.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc/3.0/), which permits non-commercial reuse, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com.

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Figure 4. — Dependence of methylation rate on BcgI concentration. (a) Reactions, at 37°C in buffer M, contained the HM oligoduplex (300 nM) and BcgI RM protein at one of the following concentrations: 10 nM, white circles; 20 nM, black circles; 40 nM, white squares; 60 nM (data from Figure 3), black squares; 100 nM, white triangles. Samples were withdrawn from the reaction at the times indicated and stopped immediately, prior to measuring the incorporation of the radiolabel into the DNA as in the ‘Materials and Methods’ section. Each data point is the mean of three repeats (error bars mark standard deviations) and the line drawn through the sets of mean values at each concentration (noted in nM next to each line) is the best fit of that data to an exponential function. (b) The first-order rate constants from the fits in (a) are plotted against the enzyme concentration; the inset shows the same data re-plotted against the square of the enzyme concentration. Error bars mark standard errors on the rate constants.

Inline graphic — Dependence of methylation rate on BcgI concentration. (a) Reactions, at 37°C in buffer M, contained the HM oligoduplex (300 nM) and BcgI RM protein at one of the following concentrations: 10 nM, white circles; 20 nM, black circles; 40 nM, white squares; 60 nM (data from Figure 3), black squares; 100 nM, white triangles. Samples were withdrawn from the reaction at the times indicated and stopped immediately, prior to measuring the incorporation of the radiolabel into the DNA as in the ‘Materials and Methods’ section. Each data point is the mean of three repeats (error bars mark standard deviations) and the line drawn through the sets of mean values at each concentration (noted in nM next to each line) is the best fit of that data to an exponential function. (b) The first-order rate constants from the fits in (a) are plotted against the enzyme concentration; the inset shows the same data re-plotted against the square of the enzyme concentration. Error bars mark standard errors on the rate constants.