The precipitation of two transport proteins, cytochrome c and hemoglobin, was carried out by using di‐(2‐ethylhexyl) sulfosuccinate, known as aerosol‐OT (AOT), as a precipitating agent. The percent precipitation was 100% when the molar ratio between AOT and the targeted protein was 11 for cytochrome c and 30 for hemoglobin. By using acetone as a polar solvent, the maximum recovery obtained was 98% for cytochrome c and 40% for hemoglobin. The surfactant contamination in the recovered product was below the detection limit. The required usage of surfactant to purify 1 mole of targeted protein was many orders of magnitude smaller than that required for a reverse micellar extraction when using AOT. Advantages of the suggested precipitation method over the reverse micellar extraction method for protein purification are discussed.
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Shin et al. (2004) studied this question.
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