Ornithine carbamoyltransferase from Spinacea oleracea: purification and characterization

Number of the records: 1

SYSNO ASEP	0142350
Document Type	J - Journal Article
R&D Document Type	Journal Article
Subsidiary J	Ostatní články
Title	Ornithine carbamoyltransferase from Spinacea oleracea: purification and characterization
Author(s)	Bellocco, E. (IT) Di Salvo, C. (IT) Lagana, G. (IT) Galtieri, A. (IT) Ficarra, S. (IT) Kotyk, Arnošt (FGU-C) Leuzzi, U. (IT)
Source Title	Biologia Plantarum. - : Ústav experimentální botaniky AV ČR, v. v. i. - ISSN 0006-3134 Roč. 45, č. 4 (2002), s. 533-538
Number of pages	6 s.
Language	eng - English
Country	NL - Netherlands
Keywords	ornithine carbomoyltransferase ; Spinacea oleracea
Subject RIV	BE - Theoretical Physics
CEZ	AV0Z5011922 - FGU-C
Annotation	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.
Workplace	Institute of Physiology
Contact	Lucie Trajhanová, lucie.trajhanova@fgu.cas.cz, Tel.: 241 062 400
Year of Publishing	2003

Number of the records: 1