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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Expression of mouse rod photoreceptor cGMP phosphodiesterase gamma subunit in bacteria.

We expressed the gamma subunit of mouse rod photoreceptor cGMP phosphodiesterase (PDE) in the bacterial pGFX-2TK expression vector which produces a cleavable 40 kDa fusion protein. The fusion protein can be isolated in a one step procedure by affinity chromatography on glutathione beads. The yield of purified fusion protein is approximately 10 mg from 1 liter of bacterial culture, or about 3 mg of PDE gamma equivalent to the PDE gamma content of approximately 200,000 mouse retinas. Both the fusion protein and the cleaved PDE gamma, to which a short kinase domain remains attached, are biologically active, inhibiting activated PDE in a manner comparable to native PDE gamma. Immobilized PDE gamma binds transducin alpha subunit charged with GTP, PDE alpha and beta subunits, and, unexpectedly, arrestin (S-antigen).[1]


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