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. 2018 Nov 13;7(11):164. doi: 10.3390/antiox7110164

Figure 1.

Figure 1

TrxC is an atypical thioredoxin. (A) Sequence logo of TrxC proteins form cyanobacteria. TrxC proteins were identified using blast at NCBI and manually curated to retain only those with a WCGL/V/IC sequence (269 sequences). This sequences were aligned using muscle and the alignment was submitted to weblogo3 to generate the consensus sequence shown. (B) Insulin reduction assay. 3 µM of recombinant TrxA (■), TrxC (●) and TrxCL32P (▲) were incubated with insulin in the presence of 1 mM of DTT. Insulin precipitation was measured as an increase in absorbance at 650 nm. Three independent purification were assayed for TrxC and two for TrxCL32P with identical results to the one shown. (C) FBPase activation assay. Oxidased pea FBPase was preincubated for 30 min with 100 µM DTT (control), 10 mM DTT or 100 µM DTT and 3 µM of TrxA, TrxC, TrxCL32P or 30 µM GST-TrxC. Data are the mean and standard error of 3 independent assays.