• Journal of Photoscience
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• v.7 no.4
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• pp.155-159
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• 2000

[Ru(bpy)$_2$(dppz)]$^2$$^{+}$ (bpy = 2,2'-bipyridine, dppz = dipyrido[3,2-a:2',3'-c]phenazine)(RuBD), a long-lifetime metal-ligand complex displays photophysical properties including long lifetime, polarized emission, and very little background fluorescence. To further show the usefulness of this luminophore(RuBD) for probing nucleic acid dynamics, its intensity and anisotropy decays when bound to tRN $A^{val}$ were examined using frequency-domain fluorometry with a blue light-emitting diode(LED)as the modulated light source. Unexpectedly much longer mean lifetime was obtained at 4$^{\circ}C$(<$\tau$>=178.3 ns) as compared to at $25^{\circ}C$(<$\tau$>=117.0 ns), suggesting more favorable conformation of tRN $A^{val}$ for RuBD when intercalated at 4$^{\circ}C$. The anisotropy decay data showed longer rotational correlation times at 4$^{\circ}C$(52.7 and 13.0 ns) than at $25^{\circ}C$ (32.9 and 10.3 ns). The presence of two rotational correlation times suggests that RuBD reveals both local and overall rotational motion of tRN $A^{val}$. Due to long lifetime of RuBD and small size of tRN $A^{val}$, very low steady-state anisotropy values were observed, 0.048 and 0.036 at 4 and $25^{\circ}C$, respectively. However, a clear difference in the modulated anisotropy values was seen between 4 and $25^{\circ}C$. These results indicate that RuBD can be useful for studying hydrodynamics of small nucleic acids such as tRN $A^{val}$.^{val}$.>.$.>.

• Journal of Microbiology and Biotechnology
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• v.10 no.5
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• pp.612-619
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• 2000

To investigate the biochemical properties of V. mimicus metalloprotease, whose gene was isolated previously from Vibrio mimicus ATCC33653, overexpression and purification were attempted. The 1.9 kb of open reading frame was amplified by PCR from pVMC193 plasmid which ligated the VMC gene with pUC19 and introduced into Escherichia coli BL21 (DE3) using the overexpression vector, pET22b (+). The overexpressed metalloprotease (VMC) was purified with Ni-NTA column chromatography and characterized with various protease inhibitors, pHs, temperatures, and substrates. The purified VMC showed the proteolytic activity against gelatin, soluble and insoluble collagens, and synthetic peptides. Unlike the observations made with all metalloproteases originated from other Vibrio sp., the VMC did not hydrolyze the casein. The proteolytic activity was critically decreased when the VMC was treated with metal chelating reagents, such as EDTA, 2,2-bipyridine, and 1, 10-phenanthroline. In particular, the 71 kDa VMC exhibited the hemagglutinating activity against human erythrocyte. As the purified VMC was treated with $CuCl_2$ and $NiCl_2$ for the chemical modification of metal binding, the proteolytic activity and hemagglutinating activity were profoundly influenced. The multialignment analysis made on the reported Vibrio metalloproteases showed the difference of amino acid sequence similarity between the two distinctive classes of Vibrio metalloproteases.

• Applied Chemistry for Engineering
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• v.28 no.5
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• pp.597-600
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• 2017

$(C_{10}H_8N_2H)_2Cr_2O_7$ was synthesized by reacting 4,4'-bipyridine and chromium (VI) trioxide. The structure of the product was characterized with FT-IR (infrared spectroscopy) and elemental analysis. The oxidation of benzyl alcohol using $(C_{10}H_8N_2H)_2Cr_2O_7$ in various solvents showed that the reactivity increased with the increase of the solvent dielectric constant, in the order of DMF (N,N'-dimethylformamide) > acetone > chloroform > cyclohexane. In the presence of DMF, an acidic catalyst such as $H_2SO_4$ $(C_{10}H_8N_2H)_2Cr_2O_7$ oxidized benzyl alcohol (H) and its derivatives ($p-OCH_3$, $m-CH_3$, $m-OCH_3$, m-Cl, $m-NO_2$). Electron donating substituents accelerated the reaction rate, whereas electron acceptor groups retarded the reaction rate. Hammett reaction constant (${\rho}$) was -0.70 (308 K). The observed experimental data were used to rationalize the hydride ion transfer in the rate determining step.

• Bulletin of the Korean Chemical Society
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• v.7 no.2
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• pp.137-142
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• 1986

The luminescence spectra of $Ru(bpy)_3^{2+}$ in poly(methacrylic acid) (PMA) solutions varied sensitively with pH. At pH < 5.5, the emission intensity increased with pH up to 4 times, while it decreased with pH beyond the pH. The enhanced emission intensity was accompanied by blue-shift of the emission maxima as much as 15 nm. The enhancement of emission intensity was attributed to the restricted rotational mobility of ligand of the cation bound to densely coiled PMA molecules at pH < 5.5. The sharp decrease in emission intensity with increasing pH near pH 5.6 was accounted for conformational transition of the polymer to more extended structure, which was also revealed in viscosity measurement. The enhancement of emission intensity became higher as NaCl concentration of the solution increased. The binding constant of $Ru(bpy)_3^{2+}$ with two carboxylate groups of PMA was calculated as $2{\times}10^5\;M^{-1}$ in 0.1 M NaCl at pH 5.2. The pH dependence of luminescence quenching rate of $Ru(bpy)_3^{2+}$ by $Cu^{++}$ also showed maximum near pH 5, and the rate was more than $10^3$ times higher than that in water, whereas the maximum enhancement of quenching rate (about 20 times) in poly(acrylic acid) (PAA) solution occurred at pH 4.5. On the other hand, the pH dependence for neutral water soluble nitrobenzene (NB) exhibited opposite trend to that of $Cu^{++}$. The quenching constant vs pH curve for $MV^{++}$ was composite of those for $Cu^{++}$ and NB. The anomalous high quenching rate for $Cu^{++}$ in PMA solution at pH < 5.5 was attributed to the binding of $Ru(bpy)_3^{2+}$ and $Cu^{++}$ to the same region of PMA, when it conforms densely coiled structure in the pH range. The observation of mininium quenching rate for NB near pH 5.5 indicated that the $Ru(bpy)_3^{2+}$ bound to the densely coiled PMA is not accessible by NB, which is in bulk water phase. The composite nature of the pH dependence of quenching rate for $MV^{++}$ in PMA solution was attributed to the smaller binding affinity of the cation to PMA, compared to that of $Cu^{++}$. The sharp, cooperative conformational transition with pH observed in PMA was not revealed in PAA. But, the pH dependence of quenching rates in this polymer reflected increased charge density and, thus, binding of cations to the polymer, and expansion of the polymer chain with pH.

• Journal of the Korean Society of Food Science and Nutrition
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• v.21 no.3
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• pp.231-240
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• 1992

Effects of dietary protein levels on the manifestations of the toxicity of gramoxone, a bipyridine herbicide, in the liver of rats were investigated. The addition of gramoxone, with regard to the body weight and feed efficiency ratio of rats, had a move dramatic effect on animals fed a low or intermediate protein diet than for those similarly treated among rats fed a relatively high protein diet. Lipid content in the rat liver tended to increase with the addition of gramoxone into each protein diet, with the exception of the high protein-gramoxone diet. The addition of gramoxone tended to increase hepatic TBA value significantly in rats, especially among those fed the low protein-gramoxone diet or the control-gramoxone diet. Significant morphological changes, including fat changes of hepatic cells and increases in the number of Kupffer cells, were found both in rats fed the low protein diet and those fed any of the gramoxone-treated diets. fat changes within hepatic cells were found to be especially severe in rats fed the low protein-gramoxone diet. Distributions of glycogen in rat liver appeared to increase in rats fed any of the diets to which gramoxone had been added.