• Economic and Environmental Geology
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• v.29 no.6
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• pp.725-732
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• 1996

To assess soil distribution patterns of heavy metals in agricultural environments, we have measured the concentrations of six metals from surficial soils of three different groups divided on the basis of the surrounding environment: (1) soil group I-cultivated soils within the purely agricultural regions, (2) soil group II-both cultivated and uncultivated soils near various livelihood facilities, and (3) soil group III-mainly cultivated soils near major polluting sources. The mean concentrations for the three soil groups were found in the range as follows: 0.12~0.15 (Cd), 4.94~6.08 (Pb), 0.05~0.11 (Hg), 2.82~3.50 (Cu), 4.69~7.82 (Zn), and 0.36~0.78 (As) ppm. Examination of data distribution trends indicates that the concentrations determined from the relatively unpolluted soil environs (groups I and II) were comparable not only between each other but also with those reported previously in background soil environs of Korea. The concentration data for the soil group III were however found to be much higher than the rest two groups. Unlike the direct comparison of the magnitudes of concentrations, results of a regression analysis exhibited much different patterns: it was seen that the correlation patterns for soil group I were rather analogous to those of soil group III. The similarities in correlation patterns between groups I and III along with the lack of correlations in soil group II suggest that soil characteristics such as whether being cultivated or not are important factors affecting soil distributions of heavy metals.

• Korean Journal of Microbiology
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• v.20 no.3
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• pp.125-133
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• 1982

Mutational experiments were performed to imporve the cellulase productivity of Aspergillus phoenicis KU175, isolated from the southern part of Korea, as a high cellulase producer. By treatment ultra-violet light nad 4-NQO(4-Nitroquinoline-N-Oxide), mutation waas induced, and treatment ultra-violet light and 4-NQO (4-Nitroquinoline-N-Oxide), mutation was induced, and A.phoenicis KU175-115 was finally selected for its highest avicelase production. Avicelase production of the mutant was increased about 2 times compared with those of the wild strain. However, activities of other hydrolytic enzymes, such as amylase, protease and nuclease, of the mutant strain didn't show a marked difference compared with those of the nuclease, of the mutant strain didn't show a marked difference compared with the wild strain, except slight increase in ribonuclease activity and slight decrease in glucoamylase activity. Avicelases from the mutant strain selected were purified from wheat bran culture by successive salting out, followed by dialysis and column chromatography, and their charcteristics were compared with thosw of the wild strain. Avicelase was separated into three peaks in the mutant strain as well as in the case of wild strain. Avicelase II activity of the mutant strain was prominently higher than that of the wild strain, while avicelase I and III activities of those were equivalent. The optimal pH ranges and stability of avicelase II from the mutant strain were pH4-5 and pH3.5-6.0, respectively, as well as in the case of the wild strain. The optimal temperature and thermal stability of avicelase II from the mutant strain were $40{\sim}50^{\circ}C\;and\;20{\sim}55^{\circ}C$, respectively. These results were same as those of the wild strain. By the using of Eadie-Hofastee plot, $K_m\;and\;V_{max}$ of avicelase II from the mutant and the wild strain were calculated to be 2.29mg/ml and $4.84{\mu}g$ reducing sugar as glucose per min equally, from the line fitted to the data by the least square method. Activity of avicelase II from the mutant strain was slightly activated by $Mg^{++}\;but\;inhibited\;by\;Cu^{++}, \;Mn^{++}\;and\;Zn^{++}$, as well as in the case of the wild strain. Therefore, it was concluded that the mutant didn't induce the formation of another avicelase isozyme, or the changes in the properties of avicelase, but induce the changes in the productively of the same avicelase II by the action of regulatory gane.

• International Journal of Industrial Entomology and Biomaterials
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• v.22 no.2
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• pp.83-93
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• 2011

Biochemical and enzymatic characterization for extracellular protease isolated from Cordyceps militaris cultivated on rice bran medium was investigated. C militaris produced proteolytic enzymes from 10 days after inoculation, maximum enzyme production was found at 25 days. The optimum temperature and pH of proteases production was at $25^{\circ}C$ and pH 7.0, respectively. The protease activity was observed in the four peaks (Pro-I, Pro-II, Pro-III, and Pro-IV) separated through Sephadex G-100 column chromatography. The separated protease was optimally active at $25^{\circ}C$. Optimum pH of the protease was between 7 and 8. Enzyme was also stable over at $30-80^{\circ}C$. The enzyme was highly stable in a pH range of 4-9. Protease activity was found to be slightly decreased by the addition of $Mg^{2+}$, $Mn^{2+}$, $Zn^{2+}$, $Fe^{2+}$ and $Cu^{2+}$, whereas inhibited by the addition of $Ca^{2+}$ and $Co^{2+}$ Protease activity was inhibited by protease inhibitor PMSF. On the other hand, the partially purified protease was investigated on proteolytic protease activity by zymogram gel electrophoresis using three substances (casein, gelatin and fibrin). Four active bands (F-I, FII, F-III, and F-IV) of fibrin degradation were revealed on fibrin zymogram gels. Both of F-II and FIII showed caseinolytic, fibrinolytic and gelatinolytic activities in three gels. Thermostability, pH stability, and pH-thermostability of the enzyme determined the residual fibrinolytic activity also displayed on fibrin zymogram gel. The only one enzyme (F-II) displayed over a broad range of temperature at $30-90^{\circ}C$. The FII displayed fibrinolytic activity in the pH range 3-5, but was inactivated in the range of pH 6-11. The F-I and F-III showed enzyme activity in the pH range of 6-11. In the pH-thermostability, the F-II only kept fibrinolytic activity after heating at $100^{\circ}C$ for 10, 20 and 30 min at pH 3 and pH 7, respectively. On the other hand, the F-II was retained activity until heating for 10 min under pH 11 condition. By using fibrin zymogram gel electrophoresis, extracellular fibrinolytic enzyme F-II from C. militaris showed unusual thermostable under acid and neutral conditions.

• Analytical Science and Technology
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• v.9 no.4
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• pp.336-344
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• 1996

The extraction of trace cobalt, copper, nickel, cadmium, lead and zinc in urine samples of organic and alkali metal matrix into chloroform by the complex with a dithizone was studied for graphite furnace AAS determination. Various experimental conditions such as the pretreatment of urine, the pH of sample solution, and dithizone concentration in a solvent were optimized for the effective extraction, and some essential conditions were also studied for the back-extraction and digestion as well. All organic materials in 100 mL urine were destructed by the digestion with conc. $HNO_3$ 30 mL and 30% $H_2O_2$ 50 mL. Here, $H_2O_2$ was added dropwise with each 5.0 mL, serially. Analytes were extracted into 15.0 mL chloroform of 0.1% dithizone from the digested urine at pH 8.0 by shaking for 90 minutes. The pH was adjusted with a commercial buffer solution. Among analytes, cadmium, lead and zinc were back-extracted to 10.00 mL of 0.2 M $HNO_3$ from the solvent for the determination, and after the organic solvent was evaporated, others were dissolved with $HNO_3-H_2O_2$ and diluted to 10.00 mL with a deionized water. Synthetic digested urines were used to obtain optimum conditions and to plot calibration-eurves. Average recoveries of 77 to 109% for each element were obtained in sample solutions in which given amounts of analytes were added, and detection limits were Cd 0.09, Pb 0.59, Zn 0.18, Co 0.24, Cu 1.3 and Ni 1.7 ng/mL, respectively. It was concluded that this method could be applied for the determination of heavy elements in urine samples without any interferences of organic materials and major alkaline elements.

• The Korean Journal of Mycology
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• v.19 no.3
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• pp.220-225
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• 1991

Activities of the $F_1-ATPase$ purified from Lentinus edodes were stimulated by $Fe^{3+},\;Fe^{2+},\;Cd^{2+},\;Mg^{2+},\;K^{+}\;and\;Co^{2+}$ but were inhibited by $Zn^{2+},\;Ca^{2+},\;Cu^{2+}\;and\;Ni{2+}$ ion. The enzyme activities were increased 130, 65, 65, 68, 105% and 23% by the 5mM $Fe^{3+}$, 10 mM$Fe^{2+}$, 1mM $Cd^{2+}$, 5mM $Mg^{2+}$, 5mM $K^{+}$ and 5mM$Co^{2+}$ ion addition, respectively, as compared with those not added. The enzyme activities were decreased 18, 19, 27 and 30% by 10 mM $Zn^{2+}$, 10mM $Ca^{2+}$, 0.5 mM $Cu^{2+}$ and 10 mM $Ni^{2+}$ ion, respectively. Anion effects of 10 mM ${Co_3}^{2-}$, 20 mM,$CN^{-}$ 20 mM$CH_3COO^{-}$ and 20 mM ${NO_3}^{-}$ ion were inhibited to the enzyme activities of 98, 95, 70 and 50%, respectively. As increasing of ${SO_4}^{2-}$ ion concentration, the enzyme activity was stimulated and 20 mM ${SO_4}^{2-}$ ion was shown increased of 21%.

• Journal of Life Science
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• v.9 no.4
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• pp.414-422
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• 1999

Our works performed for preparation of oligosaccharides from carrageenan, seaweed polysaccharide, and one active strain for carrageenan was isolated from sea water and identified to Pseudomonas alcaligenes. Carrageenan degrading enzyme was purified from the culture fluid of isolated strain-Pseudomonas alcaligenes JCL-43, by DEAE-Cellulose, Sephadex G-100, Q-Sepharose and CM Sepharose CL-6B column chromatography. Two enzyme-F-I, F-II- was identified this purifying process, and the molecular weight of the purified carrageenase were estimated to be 23.6kDa and 30.2kDa, respectively. The optimum pH and temperature for two carrageenase activity were 7.0 and 4$0^{\circ}C$. These enzymes were stable in the pH range of 6.0~7.5 and lower than 5$0^{\circ}C$, and required 1.5% NaCl for optimum activity. And these carragennase were inhibited by metal ions such as Cu2+, Zn2+, Hg2+, but increased by Ba2+ and Ca2+, and showed specificity on -carrageenan.

• Proceedings of the Korean Society of Applied Pharmacology
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• 1994.04a
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• pp.279-279
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• 1994

Fibrinolytic proteases, piscivorase I (PI) and piscivorase II (PII), were isolated from Agkistrodon piscivorus piscivorus (eastern cotonmouth moccasin) venom using gel filtration on Bio-Gel P100 and ion-exchange chromatography on CM-Sepharose. The molecular welghts of two proteases were approximately 23400 and 29000. Their isoelectric points 6.6 and 8.5, respectively. The partial amino acid sequences of PI were characterized by tryptic digestion. PI readily cleaves the A${\alpha}$-and B${\beta}$-chaln of fibronogen, but PII rapidly cleaves A${\alpha}$-chain and more slowly the B${\beta}$-chain, They were activated by Ca$\^$2+/, Mg$\^$2+/ and Ba$\^$2+/, but inhibited by Zn$\^$2+/, Cu$\^$2+/ and Mn$\^$2+/. Two enzymes were also inhibited by cysten, ${\beta}$-mercapto -ethanol, and by metal chelators such as EDTA and EGTA, but not by benzamidine, PMSF, soybean trypsin inhibitor and aprotinin. They did not act like thrombin, plasmin and kallikrein, using specific chromogenllc substrates. Two protease did not induce platelet aggregation. PI showed low hemorrhagic activity at dosage of 50 $\mu\textrm{g}$.

• Analytical Science and Technology
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• v.13 no.6
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• pp.810-814
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• 2000

The open-chain hexadentate $N_4$, $O_2$ ligands 1, 15-bis(2-hydroxybenzyl)-2, 6, 10, 14-tetraazapentadecane (BSATPD. 4HCl) has been synthesized as its tetrahydro-chloride salt and characterized by EA, IR, NMR, and Mass spectrum. Its protonation constants ($logK_n{^H}$) and stability constants ($logK_{ML}$) for $Cu^{2+}$, $Ni^{2+}$, $Co^{2+}$ and $Zn^{2+}$ ions were determined in aqueous solution by potentiometry and compared with those of analogous $N_4$, $O_2$ ligands contain ethtylenic spacers or propylenic spacers, which make six-membered chelate rings between the aliphatic nitrogen atoms.

• Korean Journal of Plant Resources
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• v.3 no.2
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• pp.115-121
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• 1990

In view of the results to have measured metallic elements which is included in 40 sorts of herb medicines and surveyed their distribution, ninekinds of metals including Co, Ce, Ga, 71, Cd, As, Sbr Bu. Pb, are never orlittle included in almost herb medicines. Other twenty four sorts of ele-ments (Mo, Sc, Be, V, Ni, Su, Se, Ba, Cr, Su, Ti, B, Li, Mg, Ca, Sr, Mnl Fe,Cu, Zn. p, Al, Na, K) are metals that are included in large quentities incomparison with others. Selagirellae Radix contains is kinds of metallicelements more then other herb medicines does. The content of elements ofinorganic metal differs greatly according to the part of herb medicines .

• YAKHAK HOEJI
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• v.4 no.1
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• pp.8-11
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• 1959

The method for the estimation of trace elements in hair is studied on this paper modifying the circular paper chromatography method shown by Giri and Balakrishnan for the estimation of vitamins from the multivitamin preparation. The elements studied are Ni, Al, Mn, Mg, Zn, Ca, Co, Cu, and Fe. The content of the element is estimated quantitatively by comparison the size and the color density of spots of the standard chromatogram prepared by the known amount of each standard substance and the chromatogram prepared from sample solution, after checking those chromatogram qualitatively. The comparative study has been made between the results from this method and the results from the other methods which are applying routinely at this laboratories. The experimental errors at each elements were within 10% limits. There was no interference between each elements. It is recommendable that this method can be applied to treat numerous speciemens saving times within experimental error of 10%.