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Ganjali, M.R.,Norouzi, P.,Alizadeh, T.,Salavati-Niasari, M. Korean Chemical Society 2007 Bulletin of the Korean Chemical Society Vol.28 No.1
A new PVC membrane potentiometric sensor that is highly selective to Hg2+ ions was prepared, using bis(2-hydroxybenzophenone) butane-2,3-dihydrazone (HBBD) as an excellent hexadendates neutral carrier. The sensor works satisfactorily in the concentration range of 1.0 × 10-6 to 1.0 × 10-1 mol L-1 (detection limit 4 × 10-7 mol L-1) with a Nernstian slope of 29.7 mV per decade. This electrode showed a fast response time (~8 s) and was used for at least 12 weeks without any divergence. The sensor exhibits good Hg2+ selectivity for a broad range of common alkali, alkaline earth, transition and heavy metal ions (lithium, sodium, potassium, magnesium, calcium, copper, nickel, cobalt, zinc, cadmium, lead and lanthanum). The electrode response is pH independent in the range of 1.5-4.0. Furthermore, the developed sensor was successfully used as an indicator electrode in the potentiometric titration of mercury ions with potassium iodide and the direct determination of mercury in some binary and ternary mixtures.
M. R. Ganjali*,P. Norouzi,T. Alizadeh,M. Salavati-Niasari 대한화학회 2007 Bulletin of the Korean Chemical Society Vol.28 No.1
A new PVC membrane potentiometric sensor that is highly selective to Hg2+ ions was prepared, using bis(2-hydroxybenzophenone) butane-2,3-dihydrazone (HBBD) as an excellent hexadendates neutral carrier. The sensor works satisfactorily in the concentration range of 1.0 10-6 to 1.0 10-1 mol L-1 (detection limit 4 10-7 mol L-1) with a Nernstian slope of 29.7 mV per decade. This electrode showed a fast response time (~8 s) and was used for at least 12 weeks without any divergence. The sensor exhibits good Hg2+ selectivity for a broad range of common alkali, alkaline earth, transition and heavy metal ions (lithium, sodium, potassium, magnesium, calcium, copper, nickel, cobalt, zinc, cadmium, lead and lanthanum). The electrode response is pH independent in the range of 1.5-4.0. Furthermore, the developed sensor was successfully used as an indicator electrode in the potentiometric titration of mercury ions with potassium iodide and the direct determination of mercury in some binary and ternary mixtures.
A New Approach for Thermodynamic Study on the Binding of Human Serum Albumin with Cerium Chloride
Rezaei Behbehani, G.,Divsalar, A.,Saboury, A.A.,Faridbod, F.,Ganjali, M.R. Korean Chemical Society 2009 Bulletin of the Korean Chemical Society Vol.30 No.6
Thermodynamics of the interaction between Cerium (III) chloride, $Ce^{3+}$, with Human Serum Albumin, HSA, was investigated at pH 7.0 and $27\;{^{\circ}C}$ in phosphate buffer by isothermal titration calorimetry. Our recently solvation model was used to reproduce the enthalpies of HSA interaction by $Ce^{3+}$. The solvation parameters recovered from our new model, attributed to the structural change of HSA and its biological activity. The interaction of HSA with $Ce^{3+}$ showed a set of two binding sites with negative cooperativity. $Ce^{3+}$ interacts with multiple sites on HSA affecting its biochemical and biophysical properties.
A New Approach for Thermodynamic Study on the Binding of Human Serum Albumin with Cerium Chloride
G. Rezaei Behbehani,A. Divsalar,A. A. Saboury,F. Faridbod,M. R. Ganjali 대한화학회 2009 Bulletin of the Korean Chemical Society Vol.30 No.6
Thermodynamics of the interaction between Cerium (III) chloride, Ce3+, with Human Serum Albumin, HSA, was investigated at pH 7.0 and 27 oC in phosphate buffer by isothermal titration calorimetry. Our recently solvation model was used to reproduce the enthalpies of HSA interaction by Ce3+. The solvation parameters recovered from our new model, attributed to the structural change of HSA and its biological activity. The interaction of HSA withCe3+ showed a set of two binding sites with negative cooperativity. Ce3+ interacts with multiple sites on HSA naffecting its biochemical and biophysical properties
Electrochemical Behavior of Redox Proteins Immobilized on Nafion-Riboflavin Modified Gold Electrode
S. Rezaei-Zarchi,A. A. Saboury*,J. Hong,P. Norouzi,A. B. Moghaddam,H. Ghourchian,M. R. Ganjali,A. A. Moosavi-Movahedi,A. Javed,A. Mohammadian 대한화학회 2007 Bulletin of the Korean Chemical Society Vol.28 No.12
Electron transfer of a redox protein at a bare gold electrode is too slow to observe the redox peaks. A novel Nafion-riboflavin functional membrane was constructed during this study and electron transfer of cytochrome c, superoxide dismutase, and hemoglobin were carried out on the functional membrane-modified gold electrode with good stability and repeatability. The immobilized protein-modified electrodes showed quasi-reversible electrochemical redox behaviors with formal potentials of 0.150, 0.175, and 0.202 V versus Ag/AgCl for the cytochrome c, superoxide dismutase and hemoglobin, respectively. Whole experiment was carried out in the 50 mM MOPS buffer solution with pH 6.0 at 25 oC. For the immobilized protein, the cathodic transfer coefficients were 0.67, 0.68 and 0.67 and electron transfer-rate constants were evaluated to be 2.25, 2.23 and 2.5 s-1, respectively. Hydrogen peroxide concentration was measured by the peroxidase activity of hemoglobin and our experiment revealed that the enzyme was fully functional while immobilized on the Nafion-riboflavin membrane.
Electrochemical Behavior of Redox Proteins Immobilized on Nafion-Riboflavin Modified Gold Electrode
Rezaei-Zarchi, S.,Saboury, A.A.,Hong, J.,Norouzi, P.,Moghaddam, A.B.,Ghourchian, H.,Ganjali, M.R.,Moosavi-Movahedi, A.A.,Javed, A.,Mohammadian, A. Korean Chemical Society 2007 Bulletin of the Korean Chemical Society Vol.28 No.12
Electron transfer of a redox protein at a bare gold electrode is too slow to observe the redox peaks. A novel Nafion-riboflavin functional membrane was constructed during this study and electron transfer of cytochrome c, superoxide dismutase, and hemoglobin were carried out on the functional membrane-modified gold electrode with good stability and repeatability. The immobilized protein-modified electrodes showed quasireversible electrochemical redox behaviors with formal potentials of 0.150, 0.175, and 0.202 V versus Ag/AgCl for the cytochrome c, superoxide dismutase and hemoglobin, respectively. Whole experiment was carried out in the 50 mM MOPS buffer solution with pH 6.0 at 25 oC. For the immobilized protein, the cathodic transfer coefficients were 0.67, 0.68 and 0.67 and electron transfer-rate constants were evaluated to be 2.25, 2.23 and 2.5 s?1, respectively. Hydrogen peroxide concentration was measured by the peroxidase activity of hemoglobin and our experiment revealed that the enzyme was fully functional while immobilized on the Nafion-riboflavin membrane.