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CPOX  -  coproporphyrinogen oxidase

Gallus gallus

 
 
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Anatomical context of CPOX

 

Associations of CPOX with chemical compounds

References

  1. An effective chromatographic separation of chicken red blood cell coproporphyrinogen oxidase and uroporphyrinogen decarboxylase, two enzymes in heme biosynthesis. Jones, M.A., Taneja, M., Xu, Y., Chung, W., Stob, C.M., Lash, T.D. Bioorg. Med. Chem. Lett. (2004) [Pubmed]
  2. Comparison of two assay methods for activities of uroporphyrinogen decarboxylase and coproporphyrinogen oxidase. Jones, M.A., Thientanavanich, P., Anderson, M.D., Lash, T.D. J. Biochem. Biophys. Methods (2003) [Pubmed]
  3. Metabolism of analogues of coproporphyrinogen-III with modified side chains: implications for binding at the active site of coproporphyrinogen oxidase. Lash, T.D., Kaprak, T.A., Shen, L., Jones, M.A. Bioorg. Med. Chem. Lett. (2002) [Pubmed]
  4. Patterns of porphyrin accumulation in response to chemicals in chick embryo liver cells. Marks, G.S., Follows, S.B., Zelt, D.T., Cole, S.P. Can. J. Physiol. Pharmacol. (1983) [Pubmed]
  5. Kinetic studies of novel di- and tri-propionate substrates for the chicken red blood cell enzyme coproporphyrinogen oxidase. Jones, M.A., He, J., Lash, T.D. J. Biochem. (2002) [Pubmed]
  6. Effect of covalent modification on coproporphyrinogen oxidase from chicken red blood cells. Jones, M.A., Hamilton, M.L., Lash, T.D. Prep. Biochem. Biotechnol. (1997) [Pubmed]
 
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