Biochemical characterization of mouse microsomal prostaglandin E synthase-1 and its colocalization with cyclooxygenase-2 in peritoneal macrophages.

@article{Lazarus2002BiochemicalCO,
  title={Biochemical characterization of mouse microsomal prostaglandin E synthase-1 and its colocalization with cyclooxygenase-2 in peritoneal macrophages.},
  author={Michael Lazarus and Bruno Kilunga Kubata and Naomi Eguchi and Yasushi Fujitani and Yoshihiro Urade and Osamu Hayaishi},
  journal={Archives of biochemistry and biophysics},
  year={2002},
  volume={397 2},
  pages={336-41}
}
We cloned the cDNA for mouse microsomal prostaglandin (PG) E synthase-1 (mPGES-1) and expressed the recombinant enzyme in Escherichia coli. The membrane fraction containing recombinant mPGES-1 catalyzed the isomerization of PGH2 to PGE2 in the presence of GSH with K(m) values of 130 microM for PGH2 and 37 microM for GSH, a turnover number of 600 min(-1), and a k(cat)/K(m) ratio of 4.6 min(-1) microM(-1). Recombinant mPGES-1 was purified and used to generate a polyclonal antibody highly specific… CONTINUE READING

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