Expression, purification and kinetic characterization of wild-type human ornithine transcarbamylase and a recurrent mutant that produces 'late onset' hyperammonaemia.

@article{Morizono1997ExpressionPA,
  title={Expression, purification and kinetic characterization of wild-type human ornithine transcarbamylase and a recurrent mutant that produces 'late onset' hyperammonaemia.},
  author={Hiroki Morizono and Mendel Tuchman and Basavapatna S. Rajagopal and Mark T McCann and Chad D Listrom and Xiaoling Yuan and Divya Venugopal and George Barany and Norma M. Allewell},
  journal={The Biochemical journal},
  year={1997},
  volume={322 ( Pt 2)},
  pages={625-31}
}
Ornithine Transcarbamylase Deficiency, an X-linked disorder, is the most common cause of inherited urea cycle disorders. Approx. 90 mutations that produce reduced levels of ornithine transcarbamylase (OTCase) activity have been identified in patients [Tuchman (1993) Hum. Mutat. 2, 174-178; Tuchman and Plante (1995) Hum. Mutat. 5, 293-295]. A model of the three-dimensional structure of OTCase, developed on the basis of its homology to the catalytic subunit of Escherichia coli aspartate… CONTINUE READING
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Synthesis 5, 403–404

  • P. F. Alewood, R. B. Jones, N. J. Hoogenraad, T. Sutherland
  • Tetrahedron Lett. 9,
  • 1984

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