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

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Biochemical and biological activities of recombinant S1 subunit of pertussis toxin.

degP-deficient strains of Escherichia coli grown in M-9 medium supplemented with ZnCl2 expressed the recombinant S1 subunit of pertussis toxin (rS1) in a form electrophoretically identical to the authentic S1 subunit. Subcellular fractionation showed that the full-length form of rS1 was membrane associated, while proteolytic fragments of rS1 were present in the periplasm. rS1 was extracted from outer membrane preparations with 8 M urea and purified by gel filtration chromatography. Purified rS1 ADP-ribosylated transducin at a similar molar efficiency relative to authentic pertussis toxin and, when associated with the native B oligomer of pertussis toxin, elicited Chinese hamster ovary cell clustering.[1]

References

  1. Biochemical and biological activities of recombinant S1 subunit of pertussis toxin. Barbieri, J.T., Pizza, M., Cortina, G., Rappuoli, R. Infect. Immun. (1990) [Pubmed]
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