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![[Figure 1]](rr5076fig1mag.jpg)
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Figure 1
Biochemical characterization of the different forms of the TaCA enzyme. (a) The elution profiles from the calibrated Superdex 200 gel-filtration column for TaCA (red), oTaCA (blue) and rTaCA (green). Peaks A and B (∼69 ml; 110 kDa) correspond to the tetrameric form of TaCA; peak C (∼85 ml; 30 kDa) corresponds to the monomeric form of TaCA. (b) SDS–PAGE gel. Lane 1, molecular-weight markers labelled in kDa. Lane 2, TaCA (reduced sample buffer). Lane 3, TaCA (nonreduced sample buffer). Lane 4, rTaCA (reduced sample buffer). Lane 5, rTaCA (nonreduced sample buffer). Lane 6, oTaCA (reduced sample buffer). Lane 7, oTaCA (nonreduced sample buffer). (c) The percentage of enzyme activity for the different TaCA enzyme samples (TaCA, green; oTaCA, red; rTaCA, blue) remaining after incubation for 1 h at various temperatures. The increase in activity of oTaCA is thought to be owing to optimization of folding, since its expression was in a mesophilic host. The remaining enzyme activities after incubation at the same temperatures are also shown for BCA1 as a control (orange). Enzyme activity was calculated with reference to the activity of the enzyme incubated at 30°C prior to the assay. |
![[Figure 1]](rr5076fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
