Purification and characterization of bovine hepatic uroporphyrinogen decarboxylase.

@article{Straka1983PurificationAC,
  title={Purification and characterization of bovine hepatic uroporphyrinogen decarboxylase.},
  author={J G Straka and James P. Kushner},
  journal={Biochemistry},
  year={1983},
  volume={22 20},
  pages={4664-72}
}
Uroporphyrinogen decarboxylase (EC 4.1.1.37) has been purified to homogeneity from bovine liver by using isoelectric and salt precipitations, followed by chromatography on DEAE-cellulose, phenyl-Sepharose, hydroxylapatite, and Sephacryl S-200. The purified enzyme is a monomer with an Mr approximately 57 000 and an isoelectric point at pH 4.6. Enzyme activity is optimal in buffers having an ionic strength of approximately 0.1 M and a pH of 6.8. The purified enzyme has a specific activity… CONTINUE READING

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