Ornithine Carbamoyltransferase from Spinacea oleracea: Purification and Characterization
作者： E. Bellocco , C. Salvo , G. Lagana , A. Galtieri , S. Ficarra
关键词: Carbamoyl phosphate synthetase 、 Gel electrophoresis 、 Chemistry 、 Dissociation constant 、 Carbamoyl phosphate 、 Michaelis–Menten kinetics 、 Ornithine 、 Chromatography 、 Ornithine Carbamoyltransferase 、 Enzyme kinetics
摘要: Ornithine carbamoyltransferase (OCT) from spinach (Spinacea oleracea L.) was purified to homogeneity and studied for some kinetic structural properties. The enzyme showed a specific activity of 436 U mg−1, its molecular mass approximately 118 kDa as estimated by Sephacryl S-200 gel filtration chromatography, the protein ran single band 38 in sodium dodecyl sulfate-polyacryamide electrophoresis. catalyses an ordered bi-bi-sequential reaction which carbamoyl phosphate binds first, followed L-ornithine; L-citrulline leaves phosphate. Michaelis constant 0.19 mM L-ornithine 13.1 µM phosphate; dissociation complex 19 µM. Km decreases pH 6.0 10.4. is heat-labile, but it protected thermal inactivation substrates; more ornithine alone than two substrates acting together.
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