Purification and characterization of recombinant human cyclooxygenase-2.

@article{Percival1994PurificationAC,
  title={Purification and characterization of recombinant human cyclooxygenase-2.},
  author={Maida Percival and Marc Ouellet and Christopher John Vincent and James A. Yergey and Brian P. Kennedy and G. Patrick O'Neill},
  journal={Archives of biochemistry and biophysics},
  year={1994},
  volume={315 1},
  pages={
          111-8
        }
}
Recombinant human cyclooxygenase-2 (hCox-2, Prostaglandin G/H synthase-2) has been purified from baculovirus-Sf9 and vaccina virus-Cos-7 cell expression systems. The detergent-solubilized, purified enzyme is heterogeneous in terms of its glycosylation. The vaccinia virus hCox-2 is a mixture of two glycoforms, whereas baculovirus hCox-2 comprises at least four species. The specific cyclooxygenase activities of both enzymes are 43 mumol O2/min/mg with arachidonic acid which is within the range of… CONTINUE READING
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