Ornithine carbamoyltransferase from Spinacea oleracea: purification and characterization

0142350 - FGU-C 20020075 RIV NL eng J - Journal Article
Bellocco, E. - Di Salvo, C. - Lagana, G. - Galtieri, A. - Ficarra, S. - Kotyk, Arnošt - Leuzzi, U.
Ornithine carbamoyltransferase from Spinacea oleracea: purification and characterization.
Biologia Plantarum. Roč. 45, č. 4 (2002), s. 533-538. ISSN 0006-3134. E-ISSN 1573-8264
Institutional research plan: CEZ:AV0Z5011922
Keywords : ornithine carbomoyltransferase * Spinacea oleracea
Subject RIV: BE - Theoretical Physics
Impact factor: 0.583, year: 2002

Ornithine c arbamoyltransferase purified from spinach had a molar mass 118 kDa and catalyzed an ordered bi-bi-sequential reaction in which carbamoyl phosphate bound first (Michaelis constant 0.013 mM) followed by ornithine (Michaelis constant 0.19 mM). The enzyme was heat-labile but was protected by substrate binding.
Permanent Link: http://hdl.handle.net/11104/0040056