Isolation of pertussis toxin subunit proteins by reverse-phase high-performance liquid chromatography and reconstitution of the holotoxin molecule.

@article{Yamakawa1990IsolationOP,
  title={Isolation of pertussis toxin subunit proteins by reverse-phase high-performance liquid chromatography and reconstitution of the holotoxin molecule.},
  author={Yoshio Yamakawa and Hiromi Sato and Yasunori Sato},
  journal={Analytical biochemistry},
  year={1990},
  volume={185 1},
  pages={176-81}
}
Reverse-phase high-performance liquid chromatography on a column of trimethylsilylated silica gel (TSK-TMS 250) was utilized for the isolation of the subunit proteins of pertussis toxin (PT). Recovery up to 95% was obtained for each of the five distinct subunits with a high degree of homogeneity as revealed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. None of the individual subunit proteins exhibited PT-related leukocytosis-promoting activity or the ability to bind haptoglobin… CONTINUE READING

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