Fig. 2: Purification and identification of the synthetic CFOR complex from T. onnurineus BCF13. | Communications Biology

Fig. 2: Purification and identification of the synthetic CFOR complex from T. onnurineus BCF13.

From: Bioconversion of CO to formate by artificially designed carbon monoxide:formate oxidoreductase in hyperthermophilic archaea

Fig. 2

a Strep-tag purified CFOR complex, Fdh3AB, and CodhAB sub-complex were loaded to a 12% acrylamide gel and stained with Coomassie Brilliant Blue after gel running. Subunits are indicated with a black arrow. M, molecular mass standards; lane 1, CFOR (6 ug); lane 2, Fdh3AB (2.2 ug); lane 3, CodhAB (3.8 ug); lane 4, Fdh3AB (2.2 ug) + CodhAB (3.8 ug). b The affinity column purified CFOR complex (blue line), and standard marker (black line) were separated on a Superdex 200 10/300 GL column. A number on a standard peak indicates: 1. Thiroglobulin, 669 kDa; 2. Apoferritin, 443 kDa; 3. Beta-amylase, 200 kDa; 4. Albumin, 66 kDa; 5. Carbonic anhydrase, 29 kDa. c The retention time versus the logarithm of the molecular weight of the CFOR complex (open rectangle) and standard marker (closed circle) was plotted on the regression.

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