• Bulletin of the Korean Chemical Society
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• v.25 no.9
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• pp.1361-1365
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• 2004

Solvatokinetic and solvatochromic behavior of bis(indolinobenzospiropyranyl) sulfide derivatives 1a-1c have been studied in various solvents. The marked negative solvatochromism is exhibited for 1a and 1b in the whole region of solvent polarity examined. Whereas, it is found only in the polar solvent region ($E_T$ > 37) for 1c. The sensitivity order to the solvent media (slope values) is 1a > 1b > 1c. The branched linear plot with a zero slope was shown for the most sterically-hindered compound 1c in the less polar-solvent region (($E_T$ < 37). The biphasic plot is indicative of dual mechanistic process, i.e., a transition state with increased zwitter-ionic character in more polar solvents and electrocyclic process with an isopolar transition state in less polar solvents.

• Korean Journal of Food Science and Technology
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• v.36 no.3
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• pp.514-517
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• 2004

O157:H7, Salmonella typhimurium, Listeria monocytogenes were treated with aqueous chlorine dioxide to elucidate effect of aqueous chlorine dioxide treatment on major food-borne pathogenic bacteria. Survival plot of E.coli O157:H7 at 5 ppm chlorine dioxide showed typical first-order rate. After 5 min of treatment, cell number decreased by 1.5 log cycle. Survival plot slope gave D value of 3.37 min. S. typhimurium and L. monocytogenes showed biphasic curve. Aqueous chlorine dioxide treatment on S. typhimurium and L. monocytogenes resulted in bactericidal effect for 5 min, and thereafter no effect was observed under experimental conditions of this study. These results suggest concentration of chlorine dioxide is more important than treatment time, and 5 ppm chlorine dioxide treatment is not sufficient for sanitizing fresh vegetables.

• Bulletin of the Korean Chemical Society
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• v.33 no.10
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• pp.3203-3207
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• 2012

The nucleophilic substitution reactions of diisopropyl chlorothiophosphate (5) with X-pyridines have been kinetically studied in MeCN at $35.0^{\circ}C$. The Hammett and Br$\ddot{o}$nsted plots for the substituent X variations in the nucleophiles show biphasic concave upwards with a break point at X = 3-Ph. The pyridinolysis rate of 5 exhibits great negative deviation from the Taft plot. A concerted $S_N2$ mechanism is proposed involving a change of the attacking direction of the X-pyridines from a frontside attack with the strongly basic pyridines to a backside attack with the weakly basic pyridines.

• Bulletin of the Korean Chemical Society
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• v.28 no.10
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• pp.1797-1802
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• 2007

The kinetics and mechanism of the nucleophilic substitution reactions of diphenyl phosphinic (1) and thiophosphinic (2) chlorides with substituted X-pyridines are investigated kinetically in acetonitrile at 35.0 and 55.0 oC, respectively. A concerted mechanism with backside nucleophilic attack is proposed for the pyridinolysis of 1, on the basis of the linear Bronsted plot with the βX value of 0.68. In the case of the pyridinolysis of 2, the Hammett and Bronsted plots are biphasic concave upwards with the break point at 3- phenyl pyridine. These results indicate a change in mechanism from a concerted SN2(P) process with direct backside nucleophilic attack for less basic nucleophiles (X = 3-CN-3-Ph) to a stepwise process with frontside attack for more basic nucleophiles (X = 4-MeO-3-Ph). Apparent secondary inverse kinetic isotope effects with deuterated pyridine (C5D5N), kH/kD < 1, are observed for the pyridinolysis of 1 and 2.

• BMB Reports
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• v.32 no.4
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• pp.326-330
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• 1999

An aspartase purified from Hafnia alvei was inactivated by diethylpyrocarbonate (DEP) in a pseudo-first-order inactivation. The first-order plot was biphasic. The inactivation process was not saturable and the second order rate constant was $1.3\;M^{-1}s^{-1}$. The inactivated aspartase was reactivated with NH₂OH. The difference absorption spectrum of DEP-inactivated vs native enzyme preparations revealed a marked peak around 242 nm. The pH dependence of the inactivation rate suggests that an amino acid residue having a pK value of 7.2 was involved in the inactivation. L-aspartate, fumarate (substrates), and chloride ion (inhibitor) protected the enzyme against inactivation, indicating that histidine residues for the enzyme activity are located at the active site of this aspartase. Inspection of the presence and absence of $Cl^-$ ion demonstrated that the number of essential histidine residues is less than two. Thus, one or two histidines are in or near the aspartate binding site and participate in an essential step of the catalytic reaction.

• Bulletin of the Korean Chemical Society
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• v.25 no.7
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• pp.1041-1045
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• 2004

Kinetic studies of the pyridinolysis $(XC_5H_4N)$ of aryl dithiomethylacetates $(CH_3CH_2C(=S)SC_6H_4Z,\;1)$ are carried out in acetonitrile at $60.0^{\circ}C$. A biphasic Bronsted plot is obtained with a change in slope from a large $({\beta}X\;{\cong}\;0.8)$ to a small $({\beta}X\;{\cong}\;0.2)$ value at $pK_a^{\circ}$ = 5.2, which is attributed to a change in the rate limiting step from breakdown to formation of a zwitterionic tetrahedral intermediate, $T^{\pm}$, in reaction path as the basicity of the pyridine nucleophile increases. This mechanism is supported by the change of the cross-interaction constant ${\rho}xz$ from a large positive ( ${\rho}xz$ = +1.36) for the weakly basic pyridines to a small negative ( ${\rho}_xz$ = -0.22) value for the strongly basic pyridines. The magnitudes of ${\rho}z$ and activation parameters are also consistent with the proposed mechanism.

• KSBB Journal
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• v.7 no.3
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• pp.201-208
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• 1992

Cell surface binding of epidermal growth factor(EGF) to EGF receptors was studied for a series of site-directed receptor mutants transfected into B82 mouse fibroblasts. Scatchard plots for truncation mutant receptors significantly lost nonlinearity for truncations below residue 1022. Transient plots of dissociation kinetics exhibited biphasic behavior for all receptor types, but the fraction of receptor in slow-dissociating form was reduced by an order of magnitude for the truncation mutants below residue 1022. Comparison of dissociation kinetics between control cells and cells treated with Triton X-100 revealed no significant variation for the slow-dissociating receptor form, but a noticeable variation was observed for the fast-dissociating receptor form when EGF receptors were truncated below residue 991. These results suggest that high affinity of EGF binding at cell surface depend on the EGF receptor cytoplasmic region.

• YAKHAK HOEJI
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• v.43 no.6
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• pp.834-842
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• 1999

The metabolism and pharmacokinetics of M-l, which is metabolite of pentoxifylline, have been studied in human liver microsomes. Biphasic kinetics was observed from the Eadie-Hofstee plot for the formation of both metabolites of M-l. For the kinetics of pentoxifylline, mean values of $V_{max1}{\;}and{\;}V_{max2}$ were 1,648 and 5,622 nmol/min/mg protein, and the estimated values of $K_{ml}{\;}and{\;}K_{m2}$ were 0.180 and 4.829 mM, respectively. For M-3, mean values of $V_{max1}{\;}and{\;}V_{max2}$ were 0.062 and 0.491 nmol/min/mg protein, and estimated values of $K_{ml}{\;}and{\;}K_{m2}$ were 0.025 and 1.216 mM. The formations of pentoxifylline and M-3 from M-1 were indentified by using several selective inhibitors of cytochrome P450 isoformes at 0.05-5 mM concentration of M-1 in human liver microsomes. For the analysis of low (0.05 mM) concentration of M-1, where the affinity was expected as low, indicated that CYPlA2 and CYP3A4 were major P450 isoforms responsible for pentoxifylline and M-3 formation. CYP3A4 and CYP2A6 appeared to be P450 isoforms responsible for M-3 formation at high (5 mM) concentration of M-1.

• Applied Biological Chemistry
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• v.24 no.3
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• pp.186-193
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• 1981

Three fractions of carboxymethyl-cellulase (F-I, F-II, and F-III) and ${\beta}-glucosidase$ form Aspergillus niger were partially purified by ammonium sulfate fractionation. Sephadex G-150 and DEAE-Sephadex column chromatography. The optimum conditions such as pH and temperature and thermal inactivation properties of the enzymes were investigated. Arrhenius plots of F-II and F-III appeared as straight lines, whereas that of F-I was biphasic. The Z-values of F-II and F-III were $8^{\circ}C$ and $10^{\circ}C$ respectively, while that of F-I was $4^{\circ}C$ over $60{\sim}70^{\circ}C$ and $383^{\circ}C$ over $70{\sim}98^{\circ}C$. Three fractions and the crude extract of carboxymethyl-cellulase exhibited a similar optimum pH 4.3 and temperature of $60^{\circ}C$, while Z-value of crude extract $(21.5^{\circ}C)$ was much higher than that of the purified enzyme. Maximum activity of both purified and crude extract of ${\beta}-glucosidase$ was shown at pH 4.7 and $60^{\circ}C$, and z-value of the enzyme was $7^{\circ}C$.