Localization, synthesis, and processing of surfactant protein SP-C in rat lung analyzed by epitope-specific antipeptide antibodies.

@article{Beers1994LocalizationSA,
  title={Localization, synthesis, and processing of surfactant protein SP-C in rat lung analyzed by epitope-specific antipeptide antibodies.},
  author={Michael F. Beers and Christina Y Kim and Chandra Dodia and Aron B. Fisher},
  journal={The Journal of biological chemistry},
  year={1994},
  volume={269 32},
  pages={20318-28}
}
Surfactant protein C (SP-C), a 3.7-kDa hydrophobic lung-specific protein, is synthesized and secreted by pulmonary type II cells through proteolytic processing of a 21-kDa propeptide (SP-C21) by currently undefined pathways. Previously, we reported the production of a polyclonal antibody against rat SP-C21 (anti-CPROSP-C) using a synthetic peptide as the immunizing antigen (Beers, M. F., Wali, A., Eckenhoff, M. E. F., Feinstein, S., Fisher, J. H., and Fisher, A. B. (1992) Am. J. Respir. Cell… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 46 extracted citations

References

Publications referenced by this paper.

Proc . Nutl . Acud . Sci . U . S . A . 87 , 2985 - 2989 Biuchim . Biophys . Acta 713 , 118 - 127 Biophys . Acta 994 , 215 - 221 Biophys

  • H. Jornvall
  • 1990

Similar Papers

Loading similar papers…