Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Odile M. Viratelle"'
Autor:
Pierre Voisin, Odile M. Viratelle, Marcelle Morrison-Bogorad, Jeanne-Marie Girault, Julie Labouesse
Publikováno v:
Journal of Neurochemistry. 60:114-127
The plasticity of astroglial glutamate and gamma-aminobutyric acid (GABA) uptakes was investigated using mouse cerebellar cell cultures. The influence of external factors, such as different sera and/or the presence of neurons, was examined. Control a
Autor:
Marc Chambon, Odile M. Viratelle
Publikováno v:
Analytical biochemistry. 263(2)
Doxorubicin, a drug largely used in chemotherapy, is transported by P-glycoprotein, a protein involved in the multidrug-resistance phenotype. Taking advantage of the doxorubicin fluorescence quenching upon interaction with DNA, a sensitive assay of t
Autor:
David Boué, Odile M. Viratelle
Publikováno v:
Biochimica et biophysica acta. 1103(1)
Phosphatidylinositol (PI) kinase activity of platelet membranes was solubilized and partially purified by anion-exchange chromatography to measure the initial enzymatic rates. Kinetic studies were performed in the presence of Triton X-100 to obtain m
Publikováno v:
Proceedings of the National Academy of Sciences. 75:1892-1896
The functional properties of CZP protein, a mutant deriving from wild-type beta-galactosidase (beta-D-galactoside galactohydrolase; EC 3.2.1.23) by a point mutation, were investigated. A large decrease of the specificity, as evaluated by the kcat/Km
Publikováno v:
Analytical Biochemistry. 144:347-355
Modifications of the cyclic AMP radioimmunoassay of Cailla et al. [in Hormones and Cell Regulation (J. Dumont and J. Nunez, eds.), Vol. 4, pp. 1–24, Elsevier/North-Holland, Amsterdam/New York (1980)] allowed its use in the determination of adenylat
Publikováno v:
Biochemical Society Transactions. 3:1006-1009
Autor:
Michael L. Sinnott, Odile M. Viratelle
Publikováno v:
Biochemical Journal. 133:81-87
1. The effect of methanol on the β-galactosidase-catalysed hydrolysis of some nitrophenyl β-d-galactopyranosides has been studied under steady-state conditions. 2. The initial fractional rate of increase of kcat. as a function of methanol concentra
Publikováno v:
European Journal of Biochemistry. 20:363-370
The “specific reactivity” of β-galactosidase from Escherichia coli for different substrates has been studied at the optimal pH value. The pH dependence of the enzyme activity has been reinvestigated in highly controlled conditions with respect t
Publikováno v:
European Journal of Biochemistry. 26:112-118
The action of Mg2+ ions on β-galactosidase activity has been studied under strictly controlled conditions with different substrates. The activation effect does not depend on the substrate. In the absence of Mg2+ ions, a residual activity has been fo
Autor:
Odile M. Viratelle, François Seydoux
Publikováno v:
Journal of molecular biology. 92(2)
A plausible extension of the two-state concerted model is proposed. This extended two-state model involves at least one state with pairwise asymmetry and consequent heterogeneous binding properties. Such a pseudoconservative transition model accounts