Mapping of the catalytic and epitopic sites of human CD38/NAD+ glycohydrolase to a functional domain in the carboxyl terminus.

@article{Hoshino1997MappingOT,
  title={Mapping of the catalytic and epitopic sites of human CD38/NAD+ glycohydrolase to a functional domain in the carboxyl terminus.},
  author={Shin-ichi Hoshino and Iwao Kukimoto and Kenji Kontani and Shin-Ichi Inoue and Yuuki Kanda and Fabio Malavasi and Toshiaki Katada},
  journal={Journal of immunology},
  year={1997},
  volume={158 2},
  pages={741-7}
}
We reported that 1) ecto-NAD+ glycohydrolase (NADase) activity induced upon differentiation of HL-60 cells is localized on the extracellular carboxyl-terminal side of CD38 and that 2) CD38 ligation by specific mAbs is followed by protein tyrosine phosphorylation in the cells. The strategy selected for identifying the relevant catalytic domains of the molecule relies upon the production in COS-7 cells of carboxyl-terminal deletion mutants of CD38. The mutants with fewer than 15 amino acids… CONTINUE READING

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