• Journal of the Korean Chemical Society
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• v.23 no.3
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• pp.161-164
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• 1979

The effect of acidity and the metal surface area of the Pd loaded zeolite catalysts; prepared from $Ca^{2+}-,\;La^{3+}-,\;NH_4^+-$exchanged Y and dealuminated HY was studied for the reaction of n-butane. The amount of strong acid site determined by the temperature programmed desorption of ammonia increased in the order NaY < CaY < LaY. Total amount of acid site decreased with increasing degree of dealumination, but the portion of strong acid site increased with increasing $SiO_2/Al_2O_3$ ratio. The effective metal surface area determined by the CO adsorption technique was large for those zeolite catalysts having strong acidity. It was found that conversion of n-butane was strongly dependent on the acidity and the effective metal surface area of the catalysts. The fact that the conversion of n-butane was proportional to the effective metal surface area suggests that the dehydrogenation by metallic component is the primary step in the reaction of n-butane.

• Korean Journal of Microbiology
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• v.37 no.3
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• pp.221-227
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• 2001

Heat shock proteins serve as chaperone by preventing the aggregation of denatured proteins and promote survival of pathogens in harsh environments. In bacteria, ethanol shock induced the major chaperone GroEL and DnaK, but in Streptococcus pneumoniae, it induced neither GroEL nor DnaK but alcohol dehydrogenase (ADH). In this study, ADH gene encoding a 104-kDa (p104) protein was identified and characterized. The deduced amino acid sequence of pneumococcal ADH shows homology with other members of the ADH family, and particularly with Entamoeba histolytica ADH2 and E. coli ADH. S. pneumoniae adh is composed of 883 amino acids and its estimated isoelectric point is 6.09. Although ADH is conserved between S. pneumoniae and E. coli, immunoblot analysis employing antisera raised against pneumococcus ADH demonstrated no cross-reactivity with ADH analog in Eschericha coli, Staphylococcus aureus and human HeLa cells. Also secretion of ADH was demonstrated by subcellular fractionation and immunoblot analysis of proteins. These results suggest that S. pneumoniae ADH could be a highly feasible candidate for both diagnostic marker and vaccine.

• Applied Chemistry for Engineering
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• v.9 no.1
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• pp.129-134
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• 1998

Conversion of propane to acrylonitrile via ammoxidation was studied using physically mixed catalysts composed of $Nb_2O_5(10{\sim}30wt%)$ and $V_{0.4}Mo_1Te_{0.1}$. Catalytic activities of ammoxidation were improved by adding strong acidic niobium oxide to $V_{0.4}Mo_1Te_{0.1}$, the selectivities to acrylonitrile+propylene being remained constant. The maximum activity was obtained at the mixing ratio 25wt% niobium oxide in $Nb_2O_5-V_{0.4}Mo_1Te_{0.1}$. Niobium oxide was found to be a selective catalyst for the oxidative dehydrogenation of propane.

• Journal of Life Science
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• v.14 no.4
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• pp.708-715
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• 2004

The lactate dehydrogenase (EC 1.1.1.27, LDH) in liver of Lempetra japonica was purified in buffer of affinity chromatography. The liver-specific $C_4$ isozyme of Gadus macrocephalus was purified by heat treatment, affinity chromatography, and DEAE-Sephacel chromatography. The liver-specific $C_4$ isozyme was eluted in a buffer containing NAD+ and was coeluted with $B_4$isozyme in plain buffer of affinity chromagraphy. Liver-specific $C_4$ isozyme in G. macrocephalus was the most thermostable, and$B_4$isozyme was more stable than $A_4$. The LDH in the fraction of pH 7.45 purified from the liver of L. iaponica by chromatofocusing was more inhibited by pyruvate than purified LDH. The optimum pH of the LDH isozyme in the liver of L. japonica was 7.5 and that of liver-specific$C_4$ isozyme was 8.5. The LDH in liver of L. japonica made complexes more with antibody against Coreoperca herzi$A_4$ and liver-specific $C_4$ than with that against eye-specific $C_4$. Therefore, the structure of the LDH in liver of L. japonica might be similarly evolved to that of subunit A and liver-specific $C_4$ isozyme in liver tissue of G. macrocephalus. The evolution rate of subunit C is faster than that of subunit A. LDH in liver of L. japonica has not one isozyme but isozymes and it was also found out to have not only subunit A and B but also subunit C.

• Journal of the Korean Chemical Society
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• v.37 no.8
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• pp.711-716
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• 1993

The mechanism for electrochemical oxidation of natural alkaloid, ${\iota}$-sparteine (SP) was studied in acetonitrile solvent. The cyclic voltammogram of SP shows two irreversible anodic peaks at +0.75 V and +1.45 V vs. Ag/AgCl (0.1M AgNO$_2$ in acetonitrile) electrode. Coulometry reveals that the number of electrons involved in each oxidation peaks is in the range of 1.2∼1.3 respectively. Neutral imine radical was produced by fast deprotonation of SP radical cation formed by oxidation of one nitrogen atom in SP. Two pathways are possible for the reaction of the neutral radical: Due to the disproportionation of the radical, SP and enamine were mainly produced. Also, the 1,2-dehydrosparteinium cation was formed as minor product through the second one electron transfer oxidation of this radical. The (+)-lupanine was produced by treatment of sparteinium cation with potassium hydroxide. We have isolated and confirmed the electrolysis products using IR, GC-MS, UV-Vis, and thin-layer spectroelectrochemical method.

• Applied Chemistry for Engineering
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• v.2 no.2
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• pp.147-154
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• 1991

Thermogravimetric measurements have been carried out to investigate the stabilization and carbonization of copolymer of acrylonitrile(95 wt %) and methyl acrylate(5 wt %) at various heating rates. The cyclization and dehydrogenation during the stabilization were important factors to determine pore development in the carbonization process. The pore and the specific surface area during the carbonization began to develope at the temperature higher than $400^{\circ}C$.

• Membrane Journal
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• v.33 no.6
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• pp.305-314
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• 2023

Various methods for removing by-products from chemical reactions are being studied to improve yield of catalytic reaction. Since the water is predominantly generated as a by-product in industrially significant reactions, it is necessary to develop the technology that can reliably remove water over a wide range of temperatures. Although several strategies using absorbents and additional dehydration reactions, have been proposed, they have limitations due to the issues such as additional energy and time consuming steps and sustainability of conversion. Membrane technology, which offers advantages such as easy operation, installation, and low maintenance costs, proves to be a promising approach for enhancing the efficiency of catalysts in various catalytic reactions. Therefore, this review discusses the removal of by-products using membranes and the associated benefits in this context.

• Journal of the Korea Academia-Industrial cooperation Society
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• v.17 no.1
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• pp.152-158
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• 2016

Glutamate is one of the major excitatory neurotransmitters in the central nervous system of vertebrates. Human GDH (hGDH) is the enzyme that regulates the glutamate metabolism and its expression is higher in the brains of schizophrenia patients than in normal subjects. This study examined the changes in the hGDH enzymatic activity caused by antipsychotic drugs (haloperidol, risperidone, (${\pm}$)-sulpride, chlopromazine hydrochloride, melperone, (${\pm}$)butaclamol, domperidone, clozapine) related to schizophrenia. First of all, hGDH isozymes (hGDH1, hGDH2) were synthesized by genetic recombination. As a result of the enzyme assay, haloperidol, (${\pm}$)-sulpride, melperone and clozapine had an inhibitory effect on the hGDH isozymes. In addition, haloperidol showed a non-competitive inhibition against the substrate, 2-oxoglutarate. In contrast, it showed an uncompetitive inhibition against another substrate, NADH. The inhibitory effect of haloperidol on hGDH2 was abolished by the presence of L-leucine, an allosteric effector of hGDH, but by not other antipsychotic drugs. These results revealed the inhibition of enzyme activity by psychotropic drugs in hGDH isoenzymes (hGDH1 and hGDH2) and the possibility that haloperidol may be used to regulate the GDH activity and glutamate concentration in the central nervous system.

• Journal of Life Science
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• v.24 no.2
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• pp.118-127
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• 2014

The kinetic properties and isozyme expression of lactate dehydrogenase (EC 1.1.1.27; LDH) in tissues from Rana catesbeiana I and II collected from February (I) and August (II) were studied. LDH activities, A4 isozyme, and LDH/citrate synthase (EC 4.1.3.7; CS) were high in skeletal muscle from R. catesbeiana I, and LDH $B_4$ isozyme increased in several tissues of R. catesbeiana II. In particular, LDH activities were high in heart and brain tissues from R. catesbeiana II. LDH eye-specific C isozyme, detected by native polyacrylamide gel electrophoresis after immunoprecipitation, was expressed in eye tissue and was more similar to the $B_4$ than $A_4$ isozyme. LDH $A_4$ isozyme was purified by oxamate-linked affinity chromatography, and the molecular weight of subunit A was 32.0 kDa. In R. catesbeiana II, levels of $Km^{PYU}$, $Vmax^{LAC}$, and tolerance to lactate of LDH were high in all tissues, and $Vmax^{PYU}$ of LDH in heart and brain tissue was highly detected. Purified $A_4$ isozyme and LDH in eye tissue were highly tolerate compared to others. The $Km^{LAC}$ value was highly measured compared to $Km^{PYU}$. The degree of inhibition by 10 mM of pyruvate on LDH activities in tissues from R. catesbeiana I and II was more pronounced as the ratio of subunit B increased. As a result, characteristic expression of LDH eye-specific C was found in R. catesbeiana. Anaerobic metabolism seemed to predominate as the LDH of skeletal muscle from I showed higher activity. It also appeared that R. catesbeiana II adapted well to incremental increases in LDH B, becoming tolerant to the lactate of LDH in tissues.

• Journal of Life Science
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• v.19 no.2
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• pp.256-263
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• 2009

The lactate dehydrogenase (EC 1.1.1.27, LDH) $A_4$ isozyme in skeletal muscle of mandrin fish (Siniperca scherzeri) was successfully purified by affinity chromatography and ultrafiltration. The molecular weight of the purified LDH $A_4$ isozyme was 140.4 kDa and its isoelectric point (pI) was 7.0. Optimal pH for enzymatic reaction was 7.5. ${K_m}^{PYR}$ and $V_{max}$ value of the purified LDH $A_4$ isozyme were $4.86{\times}10^{-5}$ M and 13.31 mM/min using pyruvate as a substrate, respectively. These kinetic properties of the purified LDH $A_4$ isozyme supported the fact that the mandrin fish was a warm-adapted species. The antibody against the purified LDH $A_4$ isozyme may be used in the metabolic physiological studies of ectothermic vertebrates and in the diagnosis of several human diseases.