Studies on uroporphyrinogen decarboxylase of etiolated Euglena gracilis Z.

@article{Juknat1989StudiesOU,
  title={Studies on uroporphyrinogen decarboxylase of etiolated Euglena gracilis Z.},
  author={A A Juknat and Andreas Seubert and Sandra Seubert and H. Ippen},
  journal={European journal of biochemistry},
  year={1989},
  volume={179 2},
  pages={423-8}
}
1. A 423-fold purified fraction of uroporphyrinogen decarboxylase (EC 4.1.1.37) showing a specific activity of 770 units/mg protein has been employed in order to study some properties in etiolated Euglena gracilis Z. 2. Uroporphyrinogen decarboxylase has a relative molecular mass of 54,000, an optimum pH of 7.2 and exhibits Michaelis-Menten kinetics, employing both uroporphyrinogen I and uroporphyrinogen III as substrates. 3. Anaerobic conditions seem not to be necessary for uroporphyrinogen… CONTINUE READING