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. 2019 Aug 23;112(4):1284–1307. doi: 10.1111/mmi.14362

Figure 5.

Figure 5

High levels of isocitrate lyase activity are present during the growth in lactate and pyruvate. A and B. Enzymatic activity of isocitrate lyase (A) and isocitrate dehydrogenase (B) measured in cell extracts of Mtb grown in lactate, pyruvate, or glucose as principal carbon source. Data represent the average and standard deviation from three independent experiments and two technical replicates for isocitrate lyase activity, and two independent experiments and two technical replicates for isocitrate dehydrogenase activity. The values at the top of the bars represent the fold‐change of the enzymatic activity detected in lactate or pyruvate vs the activity detected in glucose (minimum activity in pyruvate/lactate over maximum activity in glucose). *p value <0.00001; **p value <0.0003; ***p value <0.0002. C. Isocitrate lyase activity in cell extracts of Mtb grown in lactate, pyruvate and glucose as principal carbon source with BSA fatty acid‐free, and in medium with standard BSA but without the addition of carbon source. The data represent the average and error (average deviation) of two biological replicates. D. Growth curve in lactate, pyruvate or glucose as principal carbon source in medium supplemented with BSA fatty acid‐free, and in medium supplemented with standard BSA but no addition of carbon source.