Immunoaffinity purification and characterization of thromboxane synthase from porcine lung.

@article{Shen1986ImmunoaffinityPA,
  title={Immunoaffinity purification and characterization of thromboxane synthase from porcine lung.},
  author={R. F. Shen and Hsin H Tai},
  journal={The Journal of biological chemistry},
  year={1986},
  volume={261 25},
  pages={11592-9}
}
Thromboxane synthase has been purified 620-fold from porcine lung microsomes by a three-step purification procedure including Lubrol-PX solubilization, reactive blue-agarose chromatography, and immunoaffinity chromatography. The purified enzyme exhibited a single protein band (53,000 daltons) on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Rabbit antiserum raised against the purified enzyme immunoprecipitated thromboxane synthase activity from crude enzyme preparations of porcine… CONTINUE READING