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. 1990 Apr;58(4):999–1003. doi: 10.1128/iai.58.4.999-1003.1990

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

J T Barbieri 1, M Pizza 1, G Cortina 1, R Rappuoli 1
PMCID: PMC258573  PMID: 2108094

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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