• Resources Recycling
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• v.9 no.3
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• pp.22-28
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• 2000

A study on the recovery of gallium from zinc residues is carried out by alkali leaching using NaOH. The results show that in case of alkali leaching of zinc residues, Zn, K and Si are mainly leached out and Fe and other base metals are scarcely leached out, which results in that gallium is easily recovered by solvent extraction. The leaching efficiency of gallium increases with increasing alkali concentration and solid density. Especially, alkali consumption is considerably reduced by washing the zinc residues with water before leaching in order to eleminate the soluble zinc compounds. The gallium from zinc residues is found to be leached out with a recovery of 80% or higher for 2hrs leaching with 1~1.25 M/L NaOH solution and solid density 333 g/L at $25^{\circ}C$.

• Journal of Environmental Science International
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• v.5 no.3
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• pp.317-327
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• 1996

This study was performed to develop the biological treatment technology of wastewater polluted with heavy metals. Zinc-tolerant microorganism, such as Pseudomonas chlororaphis which possessed the ability to accumulate zinc, was isolated from industrial wastewaters polluted with various heavy metals. The characteristics of zinc accumulation in the cells, recovery of the zinc from the cells accumulating zinc, were investigated. Removal rate of zinc from the solution containing 100 mall of Zinc by zinc-tolerant microorganism was more than 90% at 48 hours after inoiulation of the microorganisms. A large number of the electron-dense granules were found mainly on thIn cell wall and membrane fractions, when determined by transmission electron microscope. Energy dispersive X- ray spectroscopy revealed that the electron-dense granules were zinc complex with the substances binding Heavy metals. The zinc accumulated into cells was not desorbed by distilled water, but more than 80% of the zinc accumulated was desorbed by 0.1M-EDTA. The residues of the cells after combustion at 55$0^{\circ}C$ amounted to about 21% of the dry weight of the cells. EDS analysis showed that the residues were comparatively pure zinc compounds containing more than 79% of zinc.

• Bulletin of the Korean Chemical Society
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• v.25 no.5
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• pp.711-714
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• 2004

Peroxynitrite enters erythrocytes through band 3 anion exchanger and oxidizes cytosolic proteins therein. As a protein associated with band 3, carbonic anhydrase II may suffer from peroxynitrite-induced oxidative damages. Esterase activity of carbonic anhydrase II decreased as the concentration of peroxynitrite increased. Neither hydrogen peroxide nor hypochlorite affected the enzyme activity. Inactivation of the enzyme was in parallel with the release of zinc ion, which is a component of the enzyme's active site. SDS-PAGE of peroxynitrite-treated samples showed no indication of fragmentation but non-denaturing PAGE exhibited new bands with lower positive charges. Western analysis demonstrated that nitration of tyrosine residues increased with the peroxynitrite concentration but the sites of nitration could not be determined. Instead MALDI-TOF analysis identified tryptophan-245 as a site of nitration. Such modification of tryptophan residues is responsible for the decrease in tryptophan fluorescence. These results demonstrate that peroxynitrite nitrates tyrosine and tryptophan residues of carbonic anhydrase II without causing fragmentation or dimerization. The peroxynitrite-induced inactivation of the enzyme is primarily due to the release of zinc ion in the enzyme's active site.

• Resources Recycling
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• v.2 no.2
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• pp.22-26
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• 1993

The flowsheet for the recovery of gallium and indium from zinc residues has been established based on the sulfuric acid treatment. In comparison with the alkali treatment, the method proposed in this work allowed the recovery of indium together with gallium. The majority of iron contained in leach liquor could be removed through the two-stage neutrallization under oxidative or reductive atmosphere. Crude gallium and indium could be obtained through the alkali and/or acid leaching of the products generated from the above treatment. In addition, cementation of indium with zinc powders could also be used for the concentration of it from weak acid solutions.

• The Korean Journal of Food And Nutrition
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• v.7 no.4
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• pp.297-306
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• 1994

This experiment was carried out to investigate the healing loss and the heavy metal residues such as copper, zinc, manganese, cadmium and lead In porcine visceras by inductively coupled argon plasma spectrometer(ICP), and to probe changes when porcine visceras were boiling In water treatment(BWT), heating in autoclave treatment (HAT) and heating In oil treatment (HOT) . The range of heating loss on porcine viscera were BWT(23.11∼34.53%) , HAT(18.48∼28.00%) and HOT(14.20∼25.22%)and the heart tissue were higher and liver were lower than those of the other tissues. The total value of heavy metal residues in large intestine, small intestine, heart, kidney, liver and stomach tissue were 11.298${\pm}$5.302 ppm, 27.825${\pm}$8. 177 ppm, 16.756${\pm}$6.334 ppm 21.107${\pm}$6.057 ppm, 25.369 ${\pm}$ 10.164 ppm and 12.611 ${\pm}$5.513 ppm, respectively. Heavy metal residues in porcine visceras tended to decrease according to heating methods and the variety viscera, and the change of total heavy metal residues on BWT, HAT and HOT were 4.16∼32.57%, 12.01∼28.09% and 9.60∼25.76%, respectively. The decrease of lead element of mean value were 21.76% and copper, zinc, manganese and cadmium element were 18.00∼ 18.16%. The change of heavy metal residues were not significant in the porcine visceras(P>0.05), and the these were significantly correlated among the three heating method(P < 0.05).

• Journal of Life Science
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• v.9 no.2
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• pp.44-48
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• 1999

The ionization of tyrosine residue is known to be involved in the stabilization of transition-state in catalysis of astacin based upon the astacin-transition state analog structure. Two tyrosine residues, Tyr-216 and Tyr-219, are conserved in all MMPs related with astacin family, We replaced Tyr-216 and Tyr-219 into phenylalanine, respectively and the zinc binding properties, kinetic parameters, and pH dependence of each mutant are determined in order to examine the role of tyrosine residue in matrilysin catalysis. Both mutants contain two zinc atoms per mol of enzyme, indicating that either tyrosime does not affect the zinc binding property of the enzyme. Y216F and Y219F mutants are highly active and the kcat/Km values are only decreased 1.1-1.5-fold compared to the wild-type enzyme. The decrease in the activity of the mutants is essentially due to the increase in Km value. The pH dependencies of the kcat/Km values for both mutants are similar to the corresponding dependencies obtained with the wild type enzyme. The pKa values at the alkaline side of both mutants are not changed. These kinetic and pH dependence results indicate that the ionization of active site tyrosine residue of matrilysin is not reflected in the kinetics of peptide hydrolysin as catalyzed by astacin.

• Journal of the Korean Magnetic Resonance Society
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• v.23 no.1
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• pp.20-25
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• 2019

The transcription factor CP2c has been recently validated as an oncogenic protein that can serve as a promising target for anticancer therapy. We have recently documented that a recombinant protein corresponding to the putative DNA-binding region (residues 63-244) of CP2c adopted two different conformers, one of which is dominated by zinc binding. However, in the present study, a longer construct encompassing residues 63-302 appeared to form a single structural domain. This domain could be considered to adopt a functionally relevant fold, as the known specific binding of a dodecapeptide to this protein was evident. Hence, the residues 63-302 region rather than 63-244 can be regarded as a natively folded structural domain of CP2c. In addition, it was confirmed that zinc ions can bind to this putative DNA-binding domain of CP2c, which resulted in reduced stability of the protein. In this context, it is suggested that the mode of action of CP2c would resemble that of tumor suppressor p53.

• Resources Recycling
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• v.9 no.3
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• pp.29-36
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• 2000

A study on the recovery of gallium from leaching solutions is carried out by solvent extraction in order to produce gallium oxide of high purity. The results show that the extraction of gallium is found to be increase with acidities of aqueous solution up to 7.4 M/L when pure isopropyl ether is used. And the extraction of iron also increases with increasing acidity of aqueous solution. It appears that the separation of gallium from iron cannot be satisfactorily accomplished with isopropyl ether. But, in the case of extaction with D2EHPA, almost complete extraction of iron is achieved-leaving all the gallium in the aqueous solution-by maintaining the acidity of aqueous solution at 2 M/L. Accordingly, $Ga_2O_3{\cdot}H_2O$ of more than 99wt.% in purity can be produced from zinc residues through the processes comprising of alkali leaching, precipitation by neutralization and solvent extraction using isopropyl ether and D2EHPA as extractants.

• Journal of Microbiology and Biotechnology
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• v.26 no.12
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• pp.2019-2029
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• 2016

Zinc finger proteins are among the most extensively applied metalloproteins in the field of biotechnology owing to their unique structural and functional aspects as transcriptional and translational regulators. The classical zinc fingers are the largest family of zinc proteins and they provide critical roles in physiological systems from prokaryotes to eukaryotes. Two cysteine and two histidine residues ($Cys_2His_2$) coordinate to the zinc ion for the structural functions to generate a ${\beta}{\beta}{\alpha}$ fold, and this secondary structure supports specific interactions with their binding partners, including DNA, RNA, lipids, proteins, and small molecules. In this account, the structural similarity and differences of well-known $Cys_2His_2$-type zinc fingers such as zinc interaction factor 268 (ZIF268), transcription factor IIIA (TFIIIA), GAGA, and Ros will be explained. These proteins perform their specific roles in species from archaea to eukaryotes and they show significant structural similarity; however, their aligned amino acids present low sequence homology. These zinc finger proteins have different numbers of domains for their structural roles to maintain biological progress through transcriptional regulations from exogenous stresses. The superimposed structures of these finger domains provide interesting details when these fingers are applied to specific gene binding and editing. The structural information in this study will aid in the selection of unique types of zinc finger applications in vivo and in vitro approaches, because biophysical backgrounds including complex structures and binding affinities aid in the protein design area.

• Resources Recycling
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• v.9 no.6
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• pp.45-52
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• 2000

Generally, the residues of EAF's dusts treated by reduction process at high temperature are disposed. If the residues can be recycled as iron sources of EAF by upgrading their iron contents, it can be expected to reduce the amounts of disposed wastes and the environmental impacts. Reduction of EAF's dusts mixed with millscale was carried out in rotary hearth furnace to upgrade iron contents of reduction residues. Dusts should be reduced rapidly to protect from reoxidation of reduced iron residue which can be reoxidized at high temperature. In our experimental conditions, optimum reduction time was about 40min. and iron contents of the residues were increased with increasing mixing ratio of millscale and upgrade to 85% at 50%wt mixing ratio. Zinc and lead contents in residues were about 3% and 0.5% respectively. The residues reduced rapidly must be recycled in EAF because heavy metal elements in the residues can be extracted easily and contaminate air and water.