• Journal of the Korean Wood Science and Technology
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• v.29 no.4
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• pp.79-88
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• 2001

Lectin was isolated from shiitake mushroom (Lentinula edodes) with 0.15 M NaCl solution, and purified by the following procedures : precipitation by ammonium sulfate, anion exchange column chromatography on DEAE Sephadex A-50 and hydroxyapatite column chromatography. The fresh pileus part of the mushroom contained more than two times of lectin compared to the stipe part, and lectins and its activity were reduced by heating. The extraction yield of crude lectin was 46.03%, 28% yield after purification on on DEAE Sephadex A-50 column chromatography. Some amino acids, aspartic acid, serine, alanine and histidine, were increased by purification process. Relatively low molecular weight parts of lectin had the agglutinating activity for rabbit blood, and its molecular weight was about 23 kDa The molecular weights of purified lectins, LA-a and LB-b, by the hydroxyapatite column chromatography were 24 kDa and 23 kDa, respectively.

• YAKHAK HOEJI
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• v.34 no.3
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• pp.215-218
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• 1990

An ion chromatographic method based on indirect photometric detection of UV transparent anions was developed. Separation of anion was accomplished on strong anion exchange column (Waters SAX) using UV detector at 254 nm. Among examined UV-active additives (Dns-H, Dns-glu, Dnsser, Dns-val), Dns-glu showed the highest sensitivity. Studies on the effects of the pH and ionic strength of eluent revealed that the increase of pH and ionic strength of the eluent decreased capacity factor. The best eluent for the separation of acetate, fluoride, chloride, nitrate and bromide was $1\;{\times}\;10^{-4}M$ Dns-glu in 5 mM phosphate buffer (pH 6.30). The detection limit of chloride ion was 2.1 ng in this condition.

• Korean Journal of Pharmacognosy
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• v.24 no.3
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• pp.203-212
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• 1993

To find antitumor components in the hot water extract of the cultured mycelia of Ganoderma lucidum, protein-bound polysaccharides were purified and fractionated (Fr. I-V) by DEAE-cellulose ion exchange column chromatography and Sepbarose CL-4B gel filtration. When a dose of 20 mg/kg/day of each was, i.p., injected into ICR mice, the inhibition ratios against the solid form of sarcoma 180 were $64.2{\sim}75.8%$. The antitumor component was examined for immunological activity. It increased the amount of superoxide anion released by induced macrophages in peritoneal cavity to 1.8 times and the count of hemolytic plaque-forming cells (PFC) was increased to 4.4 times as compared with those of the control group. It contained 68.6% polysaccharide which consisted of mannose, glucose, galactose, fucose and xylose and 5.1% protein consisting of 17 amino acids. The contents of hexosamine were 0.78%. The molecular weight of Fr. V that showed the highest antitumor activity was $5.8{\times}10^4$ dalton by Sepharose CL-4B gel filtration. It was named lucidan.

• Journal of Aquaculture
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• v.21 no.4
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• pp.285-293
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• 2008

Vitellogenin (Vg) is the precursor of vitellin (Vn), the major yolk protein of teleost fishes. In this study, Vg and Vn proteins of the Korean bullhead Pseudobagrus fulvidraco were isolated using gel-filtration chromatography (Sephadex-G 200 column) and anion-exchange chromatography (Mono Q HR 5/5 column), respectively. Purified Vn with an estimated molecular mass of 360 kDa by gel filtration chromatography was obtained from ovarian egg, and it was composited to one major subunit with an estimated molecular mass of 107 kDa by SDS-PAGE. In the result of western blotting, one major band was detected using antiserum against Vn (anti-Vn). These results suggested that Vn was composed of three subunits having the same molecular weight in Pseudobagrus fulvidraco. Vg was induced by estradiol-$17{\beta}$ ($E_2$) and purified from $E_2$ treated male serum. The molecular weight of whole Vg was estimated to be 450 kDa by gel filtration chromatography, and it is composed of three subunits with estimated molecular masses of 110 kDa, 125 kDa and 147 kDa as determined by SDS-PAGE. In the Ouchterlony's immunodiffusion test using anti-Vn and antiserum against female and male serum, purified Vg was detected in matured female and Ez treated male serum but not in untreated male. These results can be used in detecting estrogenic contamination of the aquatic environment.

• Analytical Science and Technology
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• v.28 no.3
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• pp.196-203
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• 2015

Selenium species (inorganic selenium, selenoaminoacids, and selenoproteins) were analyzed using anion exchange and affinity chromatography, which were connected to ICP/MS for the blood serum of sows fed by seleniumfortified feed. The Anion Exchange PRP X-100 column was used for the analysis of inorganic selenium (Se⁴⁺ and Se⁶⁺) and selenoaminoacids. The HEP column was used to separate SelP from GPx+SeAlb in selenoproteins. A quantitative analysis was performed using the post-column isotope dilution technique. The lactating sows were divided into three groups and fed by selenium fortified feed (organic 0.3 mg/kg, 0.6 mg/kg and inorganic 0.6 mg/kg) for four weeks. The test groups showed increases in selenoaminoacids compared with the control group, except the inorganic feed group. There was no significant difference between the organic feed groups. All test groups showed increases in selenoproteins. In particular, SelP showed a large increase that was 1.5 times higher than the other proteins.

• Microbiology and Biotechnology Letters
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• v.16 no.5
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• pp.335-342
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• 1988

An anion exchange chromatography was employed for the purification of mouse monoclonal antibodies from ascitic fluid and in vitro cultivation media. After cultivation of hybridomas, Alps 25-3, HCGK, A4W, and KW, producing IgG1, the culture supernatants were harvested by centrifugation, precipitated with 50-60％ ammonium sulfate, and dialyzed against 0.025 M Tris-HCI buffer (pH 8.2). Then the dialyzed samples were loaded into a DEAE-Trisacryl M anion exchange column. Monoclonal antibodies bound to the DEAE-Trisacryl M were eluted with 0.025 M Tris-HCI buffer (pH 8.2) containing 30-40 mM NaCl. In ammonium sulfate precipitation, the recovery of the monoclonal antibody was shown to be 90％ and 84％ from in vitro culture media containing 10％ and 2％ fetal bovine serum, respectively. On the other hand, the pretreatment by ultrafiltration enhanced the yield up to 91％ whereas the purity was lower than that by ammonium sulfate treatment. Subsequently, in the DEAE-Trisacryl M chromatographic separation, the purities and recoveries of all the monoclonal antibodies from both the in vitro culture supernatants and ascitic fluids were 70-80％ and 65％ respectively. The monoclonal antibody, Alps 25-3 could be further purified with a purity of 95％ through an immunoadsorbent chromatography.

• Journal of Dairy Science and Biotechnology
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• v.15 no.1
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• pp.1-9
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• 1997

This study was conducted to efficiently separate the Ig from Korean native cattle colostrum and to utilize them as an immunogen for the production of antibodies aginst rabbit. The results obtained were as follows : 1. About 84% of Ig G could be separated from Korean native cattle colostrum by·gel filtration using Superose 12 column on HPLC. The separation profile of Korean native cattle colostral immunoglobulin was similar that of Holstein colostral Ig. 2. Separation of Korean native cattle colostral Ig by anion exchange chromatography using Mono Q column on HPLC was poor resolution chromatographic pattern. 3. Hi-Trap Protein G column showed better results than the Protein A Sepharose CL-4B column in the Ig G binding capacity from Korean native cattle colostral Ig. 4. Protein G Sepharose Fast Flow system resulted in higher Ig g binding capacity as the industrial size scale-up approach. 5. Sufficient titer reaction of antibody to Korean native cattle colostral Ig G was confirmed by ELISA.

• Parasites, Hosts and Diseases
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• v.29 no.3
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• pp.259-266
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• 1991

In cytosolic (raction of adult Paragonimus westermani, superoxide dismutase activity was identified (4.3 units/mg of specific activity) using a xanthine-xanthine oxidase system. The enzyme was purified 150 fold in its activity using the ammonium sulfate precipitation, DEAE-Trisacryl M anion-exchange chromatography and Sephadex G-100 molecular sieve chromatography. The enzyme exhibited the enhanced activity at pH 10.0. The enzyme activity totally disappeared in 1.0mM cyanide while it remained 77.8% even in 10 mM azide. These findings indicated that the ensyme was Cu, Zn-SOD type. Molecular mass of the enzyme was estimated to be 34 kDa by gel filtration and 17 kDa on reducing SDS-polyacrylamide gel electrophoresis which indicated a dimer protein.

• Resources Recycling
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• v.30 no.4
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• pp.54-63
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• 2021

Vanadium and tungsten can be obtained by separating/recovering the leaching solution from a spent SCR DeNO_X catalyst using the soda roasting-water leaching process. Therefore, in this study, the adsorption/desorption mechanism of vanadium and tungsten in an ion-exchange column was investigated using Lewatit MonoPlus MP 600, a strong basic anion exchange resin. The operating conditions for the separation of vanadium and tungsten in the ion-exchange column was intended to present. By conducting a continuous adsorption experiment in a pH 8.5 solution, the adsorption capacity of vanadium and tungsten was found to be 44.75 and 64.92 mg/(g of resin), respectively, which showed that the adsorption capacity of tungsten was larger than that of vanadium because of the difference in ion charge. Vanadium has a higher affinity for MP 600 than tungsten. Consequently, as the vanadium-containing solution is eluted through the ion exchange resin onto which tungsten is adsorbed, the adsorbed tungsten is exchanged with vanadium and desorbed. A continuous experiment was performed with a solution of vanadium and tungsten prepared at the same concentration as the spent SCR DeNO_X catalyst leachate. The adsorption capacity of vanadium was found to be 48.72 mg/(g of resin) and 80% of the supplied vanadium was adsorbed; in contrast, almost no tungsten was adsorbed. Therefore, vanadium and tungsten were separated effectively. The ion exchange resin was treated with 2 M HCl at 15 mL/h, and 97.7% of the vanadium(99% purity) could be desorbed. After desorption, NH₄Cl was added to precipitate ammonium polyvanadate at 90℃ and recover 93% of the vanadium.

• Journal of the Korean Chemical Society
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• v.29 no.2
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• pp.178-182
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• 1985

The purpose of this study was to develop a separation method of Zn(II), Cu(II) and Mg(II), by ion exchange chromatography using cation exchange resion (Dowex 50w${\times}$8, 80-100 mesh) and anion exchange (Amberlite IRA-400). Ion exchange resions were packed into 25 ${\times}$ 2cm ID column and flow rate was controlled to 0.30 ml/min. Good eluents for separation of nonferrous metal ions such as Zn(II), Cu(II), Mg(II) were as follow: 0.5M $NaNO_3$ (pH 3.1), 0.2~0.5M HCl + 50~60% Acetone, and 1M HAc + 0.1M NaAcf(pH 3.7) aqueous solution. The mixed solution of 0.1M NaAc(pH 3.7), 0.5M HCl + 50% Acetone were found to be the best eluent for step elution. Analysis of metals were determined by atomic absorption spectrophotometer. In addition, separated Zn(II) fraction was obtained by eluted with 0.12N HCl and 1.5N $NH_4OH$ aqueous solution. This solution was titrated by the E. D. T. A.