Identification of sites for alkylation by N-ethylmaleimide and pertussis toxin-catalyzed ADP-ribosylation on GTP-binding proteins.

@article{Hoshino1990IdentificationOS,
  title={Identification of sites for alkylation by N-ethylmaleimide and pertussis toxin-catalyzed ADP-ribosylation on GTP-binding proteins.},
  author={Shin-ichi Hoshino and Shinichi Kikkawa and Kunitaro Takahashi and Hiroshi Itoh and Yoshito Kaziro and Haruhiko Kawasaki and Koji Suzuki and Toshiaki Katada and Michio Ui},
  journal={FEBS letters},
  year={1990},
  volume={276 1-2},
  pages={
          227-31
        }
}
An alpha beta gamma-trimeric GTP-binding protein (Go) serving as the substrate of pertussis toxin-(IAP) catalyzed ADP-ribosylation was purified from rat brain membranes. The constituent alpha-subunit (alpha o) was alkylated with N-ethylmaleimide (NEM), and the functionally important sulfhydryl groups were investigated. There were at least two cysteine residues highly reactive to NEM on the GDP-bound form of alpha o. These alkylations resulted in loss of its ability to be ADP-ribosylated by IAP… CONTINUE READING
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