Not so simple. Although UDP glucose dehydrogenase is normally soluble in cells, at the high concentrations of the protein you've caused to be expressed within E. coli the protein precipitates out of solution. Evidently there are weak interactions between copies of the enzyme that lead to precipitation at high concentrations but not at low concentrations.

This is a problem that must be solved, since precipitated enzyme does you no good at all. Perhaps if you changed one or more critical amino acids on the surface of the enzyme, it would no longer precipitate?

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