• 한국전기화학회:학술대회논문집
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• 한국전기화학회 1999년도 제3회 총회 및 추계학술발표회
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• pp.11-12
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• 1999

• BMB Reports
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• 제38권6호
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• pp.646-649
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• 2005

Human neuronal growth inhibitory factor (GIF), a metalloprotein classified as metallothionein-3, is specifically expressed in mammal central nervous system (CNS). In these Studies the specific antibody to human GIF was prepared and used to search the epitope of human GIF by enzyme-linked immunosorbent assay (ELISA) and sequence comparison. The result of ELISA showed the epitope of human GIF may locate on a octapeptide (EAAEAEAE) in the $\alpha$-domain of human GIF, and the result of nerve cell culture indicated that the biological activity of GIF may be affected by the specific antibody.

• Journal of Microbiology and Biotechnology
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• 제1권3호
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• pp.176-181
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• 1991

Studies on the optimum conditions for dextran production and the properties of dextransucrase (DS) were performed with Leuconostoc mesenteroides from Sikhae and Leuconostoc mesenteroides NRRL B-512(F). Dextransucrases were partially purified by lyophilization of the culture supernatant and subsequent gel chromatography on Bio-Gel A-5(m). The storage stabilities of Sikhae DS and B-512(F) DS were decreaed by the addition of dextranase. The optimum conditions for the enzyme stability were pH 5 and below $30^{\circ}C$. The B-512(F) DS lost the activity at pH 4, while Sikhae DS had 30% of the activity at the same pH. The activity of DS was decreased by EDTA. confirming the metalloprotein character of the enzymes, and was restored by the addition of calcium ions. Concanavalin A completely removed the activity of DSs, confirming the glycoprotein character of the enzymes.

• 약학회지
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• 제60권2호
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• pp.78-84
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• 2016

N-Phenylthiourea derivatives and catechol oxidase receptor complex was studied using molecular mechanics method. The starting structure was adopted from the protein databank and the calculation of energy minimization and molecular dynamics was performed with AMBER package. The molecular dynamics showed that the simulation time span of 20 ns was long enough to observe the interaction profile and stationary ligand-receptor configuration in the complex. The conformation of the ligand was related to the interaction to the receptor and the efficacy was also interpreted in this context.

• 미생물학회지
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• 제29권4호
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• pp.238-242
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• 1991

Extracellular laccase secreted from Pleurotus ostreatus was activated by $Cu^{2+}$ and $Cu^{+}$ . The enzyme was strongly inactivated by 8-hydroxyquinoline, potassium cyanide, sodium azide, sodium bisulfite and 2-mercaptoethanol. The two ionogenic groups, which have pKa values of 5.60-5.70 and 6.70-6.85 respectively, were found to relate with the active site of this enzyme. The oxidation reactions were brought about by initial single electron transfer process on the active site. The enzyme was found to be a metalloprotein which had about 3.9 cupric ions per molecule of protein as a prosthetic group. The enzyme showed a strong peak at 605 nm and a weak shoulder at 330 nm in UV-Visible absorption spectrum. Both signals disappeated upon treatment of the enzyme with 4 electron equivalent ascorbate. These results indicate that type I Cu peak and type III Cu shoulder are present in laccase.

• Journal of Microbiology and Biotechnology
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• 제24권6호
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• pp.788-794
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• 2014

An extracellular ${\beta}$-glucosidase from Aspergillus niger Au0847 was purified to homogeneity by precipitation with ammonium sulfate, anion exchange, and gel filtration. The purified protein was composed of two subunits with molecular masses of 110 and 120 kDa. Au0847 ${\beta}$-glucosidase exhibited relatively high thermostability and pH stability, and its highest activity was obtained at $65^{\circ}C$ and pH 4.6, respectively. As a potential metalloprotein, its enzymatic activity was potently stimulated by manganese ion and DTT. The ${\beta}$-glucosidase displayed avid affinity and high catalytic efficiency for geniposide. Au0847 ${\beta}$-glucosidase has potential value as an industrial enzyme for the hydrolysis of geniposide to genipin.

• Korean Chemical Engineering Research
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• 제55권4호
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• pp.556-560
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• 2017

A hemoglobin/silver nanoparticle heterolayer was fabricated for bioelectronic device with electrochemical signal-enhancement effect. As a device element, a hemoglobin, the metalloprotein, contained the heme group that showed the redox property was introduced for charge storage element. For electron transfer facilitation, a silver nanoparticle was introduced for electrochemical signal facilitation, the hemoglobin was immobilized onto Au substrate using chemical linker 6-mercaptohexanoic acid (6-MHA). Then, the silver nanoparticle was immobilized onto fabricated hemoglobin/6-MHA heterolayers by layer-by-layer (LbL) method. The surface morphology and surface roughness of fabricated heterolayer were investigated by atomic force microscopy (AFM). The redox property of hemoglobin/silver nanoparticle heterolayer was investigated by a cyclic voltammetry (CV) experiment for obtaining an oxidation potential and reduction potential. Moreover, for the assessing charge storage function, a chronoamperometry (CA) experiment was conducted to hemoglobin/silver nanoparticle-modified heterolayer electrode using oxidation and reduction potentials, respectively. Based on the results, the fabricated hemoglobin/silver nanoparticle heterolayer showed that an increased charge storage effect compared to hemoglobin monolayer-modified electrode.

• 한국패류학회지
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• 제9권2호
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• pp.16-22
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• 1993

Contamination of heavy metals in water and sediments along Mangyeong Gang(river) has reached up to critical level The object of the study is to elucidate somed molluscs which inhabit along the river on respect to the modulatory role in reducing the pollution. For the purpose, molluscs which are common in numbers and biomass in the area were collected, and Cadmim(Cd) was subjected as a reference metal in the experiment. The corresponding species were; Cipango;aludina chinensis (muddy snail) and Scapharca subcrenata (seashell). As methods, sample species were kept in laboratory under the natural condition as possible. Soil were brought from the site of the collection, dried autoclaved and wetted with ordinary water. It wad utilized as media to maintain the collected species in vitro all the way of the experiment. CdCI$^{2}$ was mixe in the medium according to experimental design. On the result obtained in the study, it is summarized that molluscs which inhabit along Mangyeong Gang(river)consume heavy mital-containing matters, so far Cd is concerned in the study. The amout of Cd concentration in tissues of the benthic natured invertebrates were dose and time related, and MT-Cd was also similar trend. Thus, Cd may eventually combine with low molecular protein forming metalloprotein, then reduce the toxicity of the heavy metal.

• Journal of Microbiology and Biotechnology
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• 제33권1호
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• pp.28-34
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• 2023

Endoribonuclease YbeY is specific to the single-stranded RNA of ribosomal RNAs and small RNAs. This enzyme is essential for the maturation and quality control of ribosomal RNA in a wide range of bacteria and for virulence in some pathogenic bacteria. In this study, we determined the crystal structure of YbeY from Staphylococcus aureus at a resolution of 1.9 Å in the presence of zinc chloride. The structure showed a zinc ion at the active site and two molecules of tricarboxylic acid citrate, which were also derived from the crystallization conditions. Our structure showed the zinc ionbound local environment at the molecular level for the first time. Molecular comparisons were performed between the carboxylic moieties of citrate and the phosphate moiety of the RNA backbone, and a model of YbeY in complex with a single strand of RNA was subsequently constructed. Our findings provide molecular insights into how the YbeY enzyme recognizes singlestranded RNA in bacteria.

• BMB Reports
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• 제40권5호
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• pp.697-707
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• 2007

Cytochrome $cbb_3$ oxidase is a member of the heme-copper oxidase superfamily that catalyses the reduction of molecular oxygen to the water and conserves the liberated energy in the form of a proton gradient. Comparison of the amino acid sequences of subunit I from different classes of heme-copper oxidases showed that transmembrane helix VIII and the loop between transmembrane helices IX and X contain five highly conserved polar residues; Ser333, Ser340, Thr350, Asn390 and Thr394. To determine the relationship between these conserved amino acids and the activity and assembly of the $cbb_3$ oxidase in Rhodobacter capsulatus, each of these five conserved amino acids was substituted for alanine by site-directed mutagenesis. The effects of these mutations on catalytic activity were determined using a NADI plate assay and by measurements of the rate of oxygen consumption. The consequence of these mutations for the structural integrity of the $cbb_3$ oxidase was determined by SDS-PAGE analysis of chromatophore membranes followed by TMBZ staining. The results indicate that the Asn390Ala mutation led to a complete loss of enzyme activity and that the Ser333Ala mutation decreased the activity significantly. The remaining mutants cause a partial loss of catalytic activity. All of the mutant enzymes, except Asn390Ala, were apparently correctly assembled and stable in the membrane of the R. capsulatus.