• Journal of the Korean Chemical Society
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• v.45 no.1
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• pp.31-39
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• 2001

Newly synthesized 15-Crown-5 derivatives including anthracene were used as neutral carriers for ion selective electrodes to determine potassium ion by potentiometry. Among the five neutral carriers studied in this work, N-(4'-benzo-15-crown-5-ether)-anthracene-9-imine was found to be the best in terms of selectivity and stability. The optimal composition of ion selective membrane was 1.0, 33.0 and 66.0 wt% for neutral carrier, PVC and plasticizer, resperctively. Addition of KTpCIPB used as a lipophilic additive improved the Nernst slope and the selectivity of potassium ion over alkali and alkaline earth metals. Especially, the selectivity of potassium ion over ammonium ion was remarkably good ($logK^{pot}_(K^+,NH_4^+}$=-2.59). The response time was also excellent ($t_{100}$=5sec) and continuous use of this electrode for three weeks has not changed the selectivity and analytical characteristics.

• Korean Journal of Environmental Agriculture
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• v.18 no.2
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• pp.148-153
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• 1999

We conducted this survey to find out the quality of ground water used for agriculture. Water samples mainly collected from plastic film houses which were located at Yongin City, Pyungtaek City, Hwasung Kun and Suwon City in Kyonggi Province. We measured EC, COD, ammonium, nitrate, sulfate, chlorite etc., and sampled three times in 1998. According to our survey, the ground water was suitable for irrigation purpose, but nitrate concentrations in ground water used in the intensive plastic film houses were high enough to require a special consideration or. the water and fertilizing management. On occasion of Pyungtaek, these results showed us specific. There are many differences among regions but aren't among periods on the part of nitrate concentrations. We found ground water quaky got worse as EC and nitrate value were going up. And there was high correlation between them.

• Journal of Microbiology and Biotechnology
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• v.10 no.6
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• pp.805-810
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• 2000

An antifungal protein antagonistic to the rice blast fungus, Pyricularia oryzae was purified from Paenibacillus macerans PM-1 by ammonium sulfate fractionation, Q Sepharose Fast Flow column chromatography, Phenyl Sepharose CL-4B column chromatography and Superose 12 gen filtration. An apparent molecular mass of the purified antifungal protein was determined as 8 kDa by SDS-PAGE and 9 kDa by analytical gel filtration, respectively, suggesting that the purified protein is a monomer. The antifungal protein was stable at pH range from 7-12 and up to $100^{\circ}C$. The protein was also stable at 0.1-1% Tween 20 and Triton X-100. The N-terminal amino acid sequence of the antifungal protein was Thr-Glu-Leu-Pro-Leu-Gly-Ile-Val-Met-Asp-Lys-Tyr-Thr-Asp-Ala-Phe-Lys-Phe-Asp-Met-Phe. Comparison of the determined sequence with other peptide and DNA sequences did not reveal homology at all. Therefore, the purified antifungal protein was speculated to be a novel protein. The condidial germination in vitro of P. oryzae KJ301:93-39 by the purified protein ($5.9{\mu} g/ml$) was limited to $9{\pm}3.2%$ only, compared with $69{\pm}2.4%$ of the control. Ungerminated conidia were swollen at basa and mid cell by the purified protein. In vivo bioassay for inhibition of conidial germination of P. oryzae KJ 301, one of the most predominating racesin Korea. the purified protein ($5.9{\mu} g/ml$)strongly inhibited the conidial germination. The conidia, even though germinated, could not develop any further to produce appressoria efficiently.

• Korean Journal of Soil Science and Fertilizer
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• v.17 no.4
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• pp.381-388
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• 1984

Addition of heavy textured red earth is being recommended to improve the texture and nutirent retention capacity of sandy soil in Korea. However, farmers are not favorable to this description because of high transportation cost and hard working. To solve this pending problem a field experiment was carried out to investigate the possibility of application of Zeolite as a foreign earth material to improve the physical and chemical characteristics of sandy soil. The experiment results suggested that Zeolite mixed with the basal N fertilizer would be substituted for other foreign earth materials in aspects of rice yield and nitrogen uptake of rice shoot. On the other hand, ammonium adsorption characteristics of soil and amendments were studied.

• Applied Biological Chemistry
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• v.24 no.4
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• pp.238-244
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• 1981

The thin Layer chromatographic determination of ${\alpha}-solanine $ in potato tuber was investigated. The solanine was extracted with methanol-chloroform mixture (2 : 1, v/v) and precipitated as the crude glycoalkaloid by the addition of ammonium hydroxide. The solanine in the crude precipitate was separated by TLC using a solvent system of 1% $NH_4OH-absolute$ ethanol-chloroform (1:2:2, v/v). The purity of ${\alpha}-solanine $ was confirmed by infrared spectrophotometry. The ${\alpha}-solanine $ separated by TLC was determined at the wavelength of 310nm after coloration with concentrated sulfuric acid-1% paraformaldehyde, with the molar absorptivity of 2,090.

• BMB Reports
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• v.33 no.2
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• pp.172-178
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• 2000

The lipoxygenase was purified 35 fold to homogeneity from the Korean red potato by an ammonium sulfate precipitation and DEAE-cellulose column chromatography. The simple purification method is useful for the preparation of pure lipoxygenase. The molecular weight of the enzyme was estimated to be 38,000 by SDS-polyacrylamide gel electrophoreses and Sepharose 6B column chromatography. The purified enzyme with 2 M $(NH_4)_2SO_4$ in a potassium phosphate buffer, pH 7.0, was very stable for 5 months at $-20^{\circ}C$. Because the purified lipoxygenase is very stable, it could be useful for the screening of a lipoxygenase inhibitor. The optimal pH and temperature for lipoxygenase purified from the red potato were found to be pH 9.0. and $30^{\circ}C$, respectively. The Km and Vmax values for linoleic acid of the lipoxygenase purified from the red potato were $48\;{\mu}M$ and $0.03\;{\mu}M$ per minute per milligram of protein, respectively. The enzyme was insensitive to the metal chelating agents tested (2 mM KCN, 1 and 10mM EDTA, and 1 mM $NaN_3$), but was inhibited by several divalent cations, such as $Cu^{++}$, $Co^{++}$ and $Ni^{++}$. The essential amino acids that were involved in the catalytic mechanism of the 5-lipoxygenase from the Korean red potato were determined by chemical modification studies. The catalytic activity of lipoxygenase from the red potato was seriously reduced after treatment with a diethylpyrocarbonate (DEPC) modifying histidine residue and Woodward's reagent (WRK) modifying aspartic/glutamic acid. The inactivation reaction of DEPC (WRK) processed in the form of pseudo-first-order kinetics. The double-logarithmic plot of the observed pseudo-first-order rate constant against the modifier concentration yielded a reaction order 2, indicating that two histidine residues (carboxylic acids) were essential for the lipoxygenase activity from the red potato. The linoleic acid protected the enzyme against inactivation by DEPC(WRK), revealing that histidine and carboxylic amino acids residues were present at the substrate binding site of the enzyme molecules.

• Korean Journal of Microbiology
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• v.30 no.3
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• pp.154-159
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• 1992

Forniation ancl ~regcncration oi' conitlial pro1oplast of Pc, ti~i.rlli~in~~~ c~rr~~culo.hryupmel.- - czllulolytic Ihngus. were examined. By using Novozyme 134(1'!/0 w/c) as a cell wall lytic enzyme. the highest yield of protopl;~sts exceeding 501%, war obtained from the qwollen conidiosporcs preincubatrd in the minimal medium containing 2-tleoxy-D-glucose(2-UC;. 75 pglml) for 10-11 11. No protoplast were obtained horn dormant spores. The regeneration frequency of the protoplasts was 49.2'!11. which was higher than that of mycclium originated protoplast (4.6-17.X1X, . in 0.6 M MgS04. pH 5.6). 'l'lie best osmotic stahilizcr ror the isoaltion and regcueration of thc protoplast was 0.6 M iimmonium sulfatc and 0.6 M magnesiuni sulfhte. respectively. 'I'lie process of the protoplast isolaiton l'ro~n swollen cnnirliospore ancl regeneration ha\, ing two pattcrns from protoplast were obsen'etl through light microscope.

• Toxicological Research
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• v.17
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• pp.97-104
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• 2001

Three types of proteases (MEF-1, MEF-2 and MEF-3) were purified from the egg cases of Ten-odera sinensis using ammonium sulfate fractionation, gel filtration on Bio-Gel P-60 and affinity chromatography on DEAE Affi-Gel blue gel. The proteases were assessed homogeneous by SDS-polyacrylamide gel electrophoresis and have molecular weight of 31,500, 32,900 and 35,600 Da, respectively. The N-terminal regions of the primary structure were compared and they were found to be different each other. MEFs readily digested the $A\alpha$ - and B$\beta$-chains of fibrinogen and more slowly the ${\gamma}$-chain. The action of the enzymes resulted in extensive hydrolysis of fibrinogen and fibrin, releasing a variety of fibrinopeptides. MEF-1 was inactivated by Cu$^{2+}$ and Zn$^{2+}$ and inhibited by PMSF and chymostatin. MEF-2 was inhibited by PMSF, TLCK. soybean trypsin inhibitor. MEF-3 was only inhibited by PMSF and chymostatin. Antiplasmin was not sensitive to MEF-1 but antithrombin III inhibited the enzymatic activity qf MEF-1. MEF-2 specifically bound to anti plasmin Among the chromogenic protease substrates, the most sensitive one to the hydrolysis of MEFs was benzoyl-Phe-Val-Arg-p-nitroanilide with maximal activity at pH 7.0 and 3$0^{\circ}C$. MEF-1 preferentially cleaved the oxidized B-chain of insulin between Leu15 and Tyr16. In contrast, MEF-2 specifically cleaved the peptide bond between Arg23 and Gly24. D-dimer concentrations increased on incubation of cross-linked fibrin with MEF-1, indicating the enzyme has a strong fibrinolytic activity.ity.

• Journal of Pharmaceutical Investigation
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• v.21 no.1
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• pp.33-41
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• 1991

A high-performance liquid chromatographic (HPLC) method was developed for the simultaneous determination of theophylline(TP) and its metabolites, 1-methyluric acid (1-MU) and 1,3-dimethyluric acid (1,3-DMU), in rat plasma and urine. An $100\;{\mu}l$ aliquot of a plasma or urine sample was mixed with $250\;{\mu}l$ of acetonitrite and vortexed. After centrifugation, $200\;{\mu}l$ (plasma) or $20\;{\mu}l$ (urine) aliquot of the supernatant was dried by $N_2$ stream and redissolved in $100\;{\mu}l$ (plasma) or $200\;{\mu}l$ (urine) of the mobile phase. A $20\;{\mu}l$ of the mobile phase solution was injected onto a $C_{18}$ reversed-phase column. The column was maintained at $45^{\circ}C$ by the aid of electric heating jacket. The mobile phase was a 3%(v/v) methanol solution in deionized water which contains sodium acetate (100 mM) and tetrabutyl ammonium hydroxide (4 mM). pH of the mobile phase was adjusted 4.5 by the addition of acetic acid. Detection limits for TP, 1-MU, and 1,3-DMU in plasma were 0.2, 0.1 and $0.1\;{\mu}/ml$, respectively and the corresponding values in urine were all $5\;{\mu}g/ml$. Inter- and intra-day variability of the assay for all compounds in the plasma samples was less than 5.5 and 3.8%, respectively. The retention times for 1-MU, 1,3-DMU, and TP were approximately 7, 8.5 and 18 min, respectively. Sample preparation procedure used in this method was simple, rapid and reproducible. Renal clearance of TP and its metabolites in rats showed plasma concentration dependency indicating renal tubular secretion and reabsorption of them.

• Journal of Microbiology and Biotechnology
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• v.16 no.11
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• pp.1753-1759
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• 2006

Paenibacillus sp. HY-8 isolated from the digestive tracts of the longicorn beetle, Moechotypa diphysis, produced an extracellular endoxylanase with a molecular weight of 20 kDa estimated by SDS-PAGE. The xylanase was purified to near electrophoretic homogeneity from the culture supernatant after ammonium sulfate precipitation, gel filtration, and ionexchange chromatography. The purified xylanase exhibited the highest activities at pH 6.0 and $50^{\circ}C$. The $K_m\;and\;V_{max}$ values were 7.2 mg/ml and 16.3 U/mg, respectively, for birchwood xylan as the substrate. Nucleotide sequence of the PCR-cloned gene was determined to have the open reading frame encoding a polypeptide of 212 amino acids. The N-terminal amino acid sequence and the nucleotide sequence analyses predicted that the precursor xylanase contained a signal peptide composed of 28 amino acids and a catalytically active 19.9-kDa peptide fragment. The deduced amino acid sequence shared extensive similarity with those of the glycoside hydrolase family 11 of xylanases from other bacteria. The predicted amino acid sequence contained two glutamate residues, previously identified as essential and conserved for active sites in other xylanases of the glycoside hydrolase family 11.