Purification and properties of porcine liver ornithine transcarbamylase.

@article{Koger1994PurificationAP,
  title={Purification and properties of porcine liver ornithine transcarbamylase.},
  author={J. B. Koger and R G Howell and Mark I Kelly and Evan E Jones},
  journal={Archives of biochemistry and biophysics},
  year={1994},
  volume={309 2},
  pages={293-9}
}
Ornithine transcarbamylase (OTCase) has been purified from porcine liver by a simple four-step procedure that included chromatography on an affinity column to which the transition-state analogue, delta-N-phosphonacetyl-L-ornithine (PALO), was covalently bound. The procedures employed yielded an enzyme which was purified some 260-fold and was judged to be homogeneous by nondenaturing- and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Apparent homogeneity of the enzyme was… CONTINUE READING

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