The high-flux/low-affinity cyanobacterial bicarbonate transporter BicA is a member of sulfate permease/solute carrier 26 (SulP/SLC26) family and plays a major role in cyanobacterial inorganic carbon uptake. In order to study this important membrane protein, robust platforms for over-expression and protocols for purification are required. In this work we have optimized the expression and purification of BicA from strain Synechocystis sp. PCC 6803 (BicA₆₈₀₃) in Escherichia coli. It was determined that expression with C43 (DE3) Rosetta2 at 37 °C produced the highest levels of over-expressed BicA₆₈₀₃ relative to other strains screened, and membrane solubilization with n-dodecyl-β-d-maltopyranoside facilitated the purification of high levels of stable and homogenous BicA₆₈₀₃. Using these expression and purification strategies, the final yields of purified BicA were 6.5 ± 1.0 mg per liter of culture.

高通量/低亲和力的蓝细菌碳酸氢盐转运蛋白BicA是硫酸盐渗透酶/溶质载体26（SulP / SLC26）家族的成员，在蓝细菌无机碳的吸收中起主要作用。为了研究这种重要的膜蛋白，需要强大的平台用于过度表达和纯化方案。在这项工作中，我们优化了菌株Synechocystis sp。中BicA的表达和纯化。大肠杆菌中的PCC 6803（BicA ₆₈₀₃）。已确定相对于筛选的其他菌株，用C43（DE3）Rosetta2在37°C的表达产生了最高水平的BicA ₆₈₀₃超表达，并用正十二烷基-β - d溶解了膜-麦芽吡喃糖苷有助于纯化高水平的稳定且均质的BicA ₆₈₀₃。使用这些表达和纯化策略，纯化的BicA的最终产量为每升培养液6.5±1.0 mg。