• Korean Journal of Veterinary Service
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• v.28 no.4
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• pp.393-405
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• 2005

In prion pathogenesis, the structural conversion of the cellular prion protein $(PrP^c)$ to its abnormal isomer $(PrP^{Sc})$ is believed to be a major event. The susceptibility or resistance to natural sheep scrapie is associated with polymorphisms of host PrP gene (PRNP) at amino acid residues 136, to a lesser extent 154. The 112 residue in ovine PrP displays a natural polymorphism, Methionine to Threonine, which has not been thoroughly investigated. However the cell-free conversion assay showed that ARQ with Thr112 $(T_{112}ARQ)^{1)}$ presents lower convertibility to $PrP^{Sc}$than wild type ARQ $(M_{112}ARQ)$ [1] In this study we generated ovine recombinant PrPs of 112 allelic variants by metal chelate affinity chromatography and cation exchange chromatography. The final purity of the ovine PrP ARQ was more than $95\%$. These variants showed similar immunoreactivity against anti-PrP monoclonal antibodies in Western blot and ELISA. The refolded $M_{112}ARQ$ and $M_{112}ARQ$ presented the secondary structural content to similar extent via CD spectroscopy analysis. The inherited structural features of $M_{112}ARQ$ and $M_{112}ARQ$ under the different biophysical conditions are in the middle of investigation.

• Applied Biological Chemistry
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• v.46 no.4
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• pp.385-390
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• 2003

An antimicrobial peptide was purified from the roots of Phytolacca americana L. and was designated as PAMP-r. Purification was carried out by DEAE-cellulose anion exchange, sephadex G-75 gel filtration, Mono S cation exchange, and Resource RPC reverse phage chromatography. The molecular weight of PAMP-r was estimated to be about 4,900 Da by 15% SDS-PAGE under reducing condition. PAMP-r exhibited a broad spectrum of antimicrobial activity. PAMP-r was stable against heat and pH treatment; its activity was not diminished by the heat treatment up to $80^{\circ}C$ for 30 min, and it showed a pH stability in the range between pH 3.0 to pH 8.0.

• Journal of Microbiology and Biotechnology
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• v.11 no.2
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• pp.337-341
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• 2001

To isolate antifungal substances from Korean radish (Raphanus Sativus L.) seeds, various purification techniques such as DE52 cellulose anion exchange, SP-Sephadex C-25 cation exchange, and Sephadex G-50 gel filtration chromatographies were used. The molecular masses of two purified R. sativus antifungal proteins (RAPs) were estimated to be about 6.1 kDa (RAP-1) and 6.2 kDa (RAP-2) by SDS-PAGE, and 5.8 kDa(RAP-1) and 6.2 kDa (RAP-2 by a gel filtration chromatography, respectively. Purified proteins RAP-1 and 2 clearly exhibited different growth inhibitory activities against other microorganisms like Candida albicans and Saccharomyces cerevisiae. Although they have similar molecular masses, both RAP-1 and 2 proteins are not identical because their microbial inhibitory actions were different. Therefore, RAP-1 could be a new antifungal protein when compared with the antifungal activities of 2S albumins, Rs-AFPs, Mj-AMPs, chitinase, glucanase, permatin, and ribosome inactivating proteins, all of which are anifungal proteins of plants.

• Korean Journal of Pharmacognosy
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• v.14 no.2
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• pp.39-43
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• 1983

Polyamine constituents of fresh Panax ginseng root and dried white ginseng were extracted with 5% trichloroacetic acid, respectively. The isolation of polyamine constituents was conducted by the cation exchange chromatography using $Dowex-50W{\times}8$ resin and the detection was performed with TLC. Identification of the polyamine was carried out by the methods of IR, NMR, MS spectroscopy and GLC. Polyamine constituents of white and fresh ginseng root were identical and composed of five different polyamines. The major polyamine in white and fresh ginseng root was determined as putrescine.

• Journal of radiological science and technology
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• v.13 no.2
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• pp.43-49
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• 1990

[ $^{111}$ ]In has wide applications in nuclear medicine for labelling and in-vivo distribution studies. A method is developed for the production of carrier free $^{111}$In using the reaction $^{nat.}Cd(p,\;xn)$ $^{111}$In with MC-50 cyclotron. Carrier free $^{111}$In was separated from the irradiated metallic cadmium by liquid-liquid extraction and cation exchange chromatography. The yield of $^{111}$In at EOB is $0.8mCi/{mu}\;Ahr$ and the nuclidic purity is over 99%. $^{111}In-DTPA\;and\;^{111}In-bleomycin$ were prepared for medical study.

• 한국생물공학회:학술대회논문집
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• 2002.04a
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• pp.500-503
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• 2002

In order to improve the physical properties of food such as texture and food self-life. Transglutaminase(mTG) from Streptoverticillum morbarense was prepared. In the preliminary experiments, presence of proteases in the crude enzyme did not improve the texture of dough, which mean the inteference of mTG reaction by the proteases. Among the cation exchange resins tested for the removal of proteases, Monoplus S 100(Bayer, Germany) was the most efficient resin with 20 fold increase in the mTG/protease activity ratio. By further purification steps with a quaternary ammonia salt resin and a gel permeation chromatography, proteases were effectively removed from the preparation. Therefore, the improvement of flour texture was shown by adding the protease-free mTG.

• Bulletin of Food Technology
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• v.17 no.3
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• pp.69-74
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• 2004

A soy protein hydrolysate was found to inhibit rat platelet aggregation induced by ADP, an aggregating agent. To find out its principal antiplatelet peptide(s), the soy protein hydrolysate was separated successively by gel filtration chromatography, revere-phase HPLC, and cation exchange HPLC. During the course of separation, we observed that most fractions had antiplatelet effects, which suggests that most peptides have some degree of antiplatelet effect. Following the inhibitory fractions, we purified and identified two new peptides, SSGE and DEE, by LC-electrospray ionization MS and peptide equencing. Both peptides were highly hydrophilic. The concentrations to obtain 50% inhibition ($IC_50$) of the aggregation intensity were approximately $\458muM$ and $\485muM$, respectively, for SSGE and DEE.

• The Korean Journal of Zoology
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• v.37 no.2
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• pp.274-280
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• 1994

담배나방(Heliothis assulta) 혈림프 항세균성 단백질의 특성을 알아보기 위해 종령 유충의 혈강으로 고라구연us thuringiens논 균을 주입하였다. 혈림프의 항세근적 활성은 주입후 48시간 경과군에서 가장 높았으며, E. coli와 풍 thuringiensis에 대하여 항세균성을 보이는 두 개의 단백질(G-1 및 G-11)들을 cation exchange chromatography와 gel filtration을 통해 정제하였다 49KD와 46KB의 두 subunit로 구성된 G-1은 높은 glvcine(17 13 mole %) 및 alanine(13.88 mole %) 함량을 보였으며, 14KD의 단일 pclvpeptide인 G-11에서는 histidine(16 14 mole %)과 glvclne(14.27 mole %)의 함량이 높아, 이러한 높은 glvcine 함량에 있어서 곤충에서 나타나는 다른 항세균성 단백질과 공통점을 보인다.

• Proceedings of the Ginseng society Conference
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• 1998.06a
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• pp.160-167
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• 1998

Chemical studies of nitrogen compounds of Panax ginseng seem relatively rare, Probably due to the isolation difficulties, subsequently the investigations of biological activities are little. The experimental conditions were established for highly complete extraction of peptides (basic, acidic and neutral) from Panax ginseng. This task was achieved by applying the follow isolation procedure: 1 , the sequential extraction with water, 0.1% TFA in 20% acetonitril and buffer pH 6.5 (water-pyridine-acetic acid 100:3:900) : 2, fractionation by ultrafiltration : 3, n-butanol extraction 4, cation- and anion-exchange chromatography : 5, chromato-electrophoresis. The comparison of red ginseng (xylem Sl pith part) and red ginseng inside white (xylem Sc pith part) was also provided. To analyze the peptide mixture the chromato-electrophoresis method of separation was applied. Optimal conditions for peptides mapping of sample were explored. Our experiments revealed the quantitative difference of peptide between xylem & pith and phloem & cortex part. We have also found the qualitative difference in the composition of polypeptides between normal red ginseng (xylem Sc pith part) and red ginseng inside-white (xylem St pith part)

• Microbiology and Biotechnology Letters
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• v.40 no.2
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• pp.163-167
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• 2012

Since D-xylose is not fermentable in Saccharomyces cerevisiae, its conversion to D-xylulose is required for its application in biotechnological industries using S. cerevisiae. In order to convert D-xylose to D-xylulose by way of an enzyme immobilized system, D-xylose isomerase (XI) of Escherichia coli was fused with 10-arginine tag (R10) at its C-terminus for the simple purification and immobilization process using a cation exchanger. The fusion protein XIR10 was overexpressed in recombinant E. coli and purified to a high purity by a single step of cation exchange chromatography. The purified XIR10 was immobilized to a cation exchanger via the electrostatic interaction with the C-terminal 10-arginine tag. Both the free and immobilized XIR10 exhibited similar XI activities at various pH values and temperatures, indicating that the immobilization to the cation exchanger has a small effect on the enzymatic function of XIR10. Under optimized conditions for the immobilized XIR10, D-xylose was isomerized to D-xylulose with a conversion yield of 25%. Therefore, the results of this study clearly demonstrate that the electrostatic immobilization of XIR10 via the interaction between the 10-arginine tag and a cation exchanger is an applicable form of the conversion of D-xylose to D-xylulose.