Functional domains of Pseudomonas aeruginosa exoenzyme S.

@article{Knight1995FunctionalDO,
  title={Functional domains of Pseudomonas aeruginosa exoenzyme S.},
  author={D A Knight and Viviane Finck-Barbançon and S M Kulich and Joseph T. Barbieri},
  journal={Infection and immunity},
  year={1995},
  volume={63 8},
  pages={3182-6}
}
Recombinant exoenzyme S (rHisExoS) of Pseudomonas aeruginosa was expressed in Escherichia coli as a soluble, cytosolic His fusion protein. rHisExoS was purified by Ni(2+)-affinity chromatography in the presence of protease inhibitors without detectable degradation. rHisExoS possessed a specific activity (within twofold) for the factor-activating exoenzyme S-dependent ADP-ribosylation of soybean trypsin inhibitor (SBTI) similar to that of native exoenzyme S. Analysis of several deletion peptides… CONTINUE READING