• Analytical Science and Technology
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• v.10 no.6
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• pp.403-407
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• 1997

Separation factor for $^6Li$ and $^7Li$ have been determined using ion exchange resin having 1,7,13-trioxa-4,10,16-triazacyclooctadecane($N_3O_3$) as an anchor group. The lighter isotope, $^6Li$ is concentrated in the solution phase, while the heavior isotope, $^7Li$ is enriched in the resin phase. By Ccolumnl chromatography[0.9cm(I.D)${\times}$20cm(height)] using 2.0M ammonium chloride solution as an eluent, single separation factor, ${\alpha}$, 1.009. i.e.$(^7Li/^6Li)_{resin}$/$(^7Li/^6Li)_{solution}$ was obtained by the Glueckauf theory from the elution curve and isotope ratios.

• Biomedical Science Letters
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• v.18 no.2
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• pp.96-103
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• 2012

Kv 4.2 ion channel protein has an ability to open at subthreshold membrane potentials and to recover quickly from inactivation. That is very important for neuronal signal transmission in vertebrate brain. In order to purify Kv 4.2 protein, the novel purification methods were experimented. The purification procedure utilized chromatography on DE-52 ion exchange column and affinity chromatography on a WGA-Sepharose 4B, and Kv 4.2 affinity column chromatography. It was found that 0.5% (wt./vol.) Triton X-100 detergent in lysis buffer worked well for Kv 4.2 protein solubilization from rat brain membrane. Protein quantitative determination was conducted by BCA method at 562 nm for each purification step to avoid determination interference of protein at 280 nm by detergent. The confirmation of Kv 4.2 existence and amount is performed using by SDS-PAGE/immunoblotting or 96-well dot blotting. The Kv 4.2 without interacting protein that contains carbohydrate, was purified from novel biochemical 3-steps purification method for further research.

• Journal of Korean Society of Occupational and Environmental Hygiene
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• v.4 no.2
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• pp.189-197
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• 1994

Analytic methods for Cr(VI) level in industrial hygienic field were suggested by the National Institute for Occupational Safety and Health(NIOSH method 7600, 7604). There were growing needs for measurement of Cr(III) and Cr(VI) levels simultaneously. Two analytical methods were suggested to determine Cr(III) and Cr(VI) levels simultaneously. The one is method by using reversed phase high peformance liquid chromatography(HPLC) and the other is by using ion exchange HPLC. The purpose of this work was to evaluate the usefulness of these two analytic methods. For the difference of ionic charges of Cr(III)-ethylendiamine tetraacetic acid(EDTA) chelate and $CrO_4{^-2}$, we could detect them simultaneously by ion exchange HPLC. Also, we attempted to determine the levels of Cr(III) and Cr(VI) chelated with sodium diethyldithiocarbamate(NaDDTC) by using reversed phase HPLC. The confirmation of Cr(III) and Cr(VI) were checked by fraction collector and nameless atomic absorption spectrometer. The optimal conditions for the formation of Cr(III)-EDTA chelate were two hours incubation period with pH 5. Cr(III)-EDTA and Cr(VI) in EDTA solution were successfully separated by anion exchange column using $Na_2CO_3/NaOH$ mixture as mobile phase. Peaks of Cr(III)-EDTA and Cr(VI) in EDTA were identified at 5 minutes and 7 minutes of retention time respectively by the ion exchange HPLC. The formation of Cr(III)-NaDDTC and Cr(VI)-NaDDTC chelates were twelve hours incubation period. Cr(III)-NaDDTC and Cr(VI)-NaDDTC chelates were separated by reversed phase column using methanol and water mixture as mobile phase. Peaks of Cr(VI)NaDDTC and Cr(III)-NaDDTC chelates were identified at 13 minutes and 26 minutes of retention time respectively by the reversed phase HPLC. Due to reduction of Cr(VI) to Cr(III), it seems to be not suitable for simultaneous determination of Cr(III)-NaDDTC and Cr(VI)-NaDDTC chelates by reversed phase HPLS. Simultaneos determination of Cr(III) and Cr(VI) by ion exchange HPLC was more accurate and simple method.

• Journal of Oral Medicine and Pain
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• v.25 no.1
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• pp.29-39
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• 2000

Lysyl Oxidase from fetal bovine aorta was purified to homogenity using extraction, Sephacryl S200HR chromatography, Hydropore AX ion-exchange high performance liquid column chromatography, Cibacron blue affinity chromatography, and Sephacryl S-300 HR chromatography in the presence of protease inhibitor. The purified enzyme was active toward lathyritic collagen as well as elastin and was sensitive to aminonitriles such as BAPN. Upon Sephacryl S-300 HR chromatography, the enzyme was eluted as a peak with a $K_{av}$ value of 0.45 (65% of $V_t$ ) and it eluted from high performance liquid ion-exchange column (Hydropore |AX) at single position (ionic strength, I = 0.1~0.15). Once purified, it showed one band upon SDS-PAGE. It migrated to a band the mobility of which corresponded to a Mr of 33,500 upon reduction while it migrated to a 24,500 Mr position under the non-reducing condition. In constrast to other reports, it is concluded that fetal bovine aorta contains only one type of lysy oxidase.

• KSBB Journal
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• v.13 no.5
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• pp.535-539
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• 1998

The monellin, a sweet-taste protein, was expressed and secreted in Saccharomyces cerevisiae. The secreted menellin was concentrated using an ultrafiltration membrane with a nominal molecular weight cut off of 3,000 or by ammonium sulfate precipitation. The monellin was purified by G-25 gel filtration chromatography, followed by CM-Sepharose ion exchange chromatography. The purified monellin was characterized by SDS-PAGE (SDS-Polyacrylamide Gel Electrophoresis) and PHLC. The molecular weight of monellin was found to be 10,700 dalton, and its purity was over 95%.

• YAKHAK HOEJI
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• v.28 no.3
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• pp.139-147
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• 1984

L-PHA, a lectin having lymphoagglutinating activity but devoid of erythroagglutinability which is contained in Korean white kidney bean (Phaseolus vulgaris L.), was isolated and purified through several techniques such as ion exchange chromatography, hydroxyapatite column and affinity chromatography. Purified L-PHA was identified as a single band by polyacrylamide disc gel electrophoresis. The molecular weight of the L-PHA was estimated about 125, 000 daltons by polyacrylamide gel electrophoresis and it was turned out having one subunit (probably dimer of the Yachnin's model) of Mr~60, 000. Immunochemical studies also tried and these results reconfirmed the purity of this L-PHA.

• Bulletin of the Korean Chemical Society
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• v.31 no.11
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• pp.3395-3398
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• 2010

• Journal of Radiopharmaceuticals and Molecular Probes
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• v.7 no.2
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• pp.69-77
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• 2021

No-carrier-added holmium-166 (n.c.a ¹⁶⁶Ho) separation is performed based on the results of separation conditions using stable isotopes dysprosium (Dy) and holmium (Ho) to minimize radioactive waste from separation optimization procedures. Successful separation of two adjacent lanthanides was achieved by cation-exchange chromatography using a sulfonated resin in the H+ form (BP-800) and α-hydroxyisobutyric acid (α-HIBA) as eluent. For the identification process after separation of stable isotopes, the use of chromogenic reagents alternatively enables on-line detection because the lanthanides are hardly absorb light in the UV-vis region or exhibit radioactivity. Four different chromogenic reagents were pre-tested to evaluate suitable coloring reagents, of which 4-(2-Pyridylazo)resorcinol is the most recommendable considering the sensitivity and specificity for lanthanides. Lanthanide radioisotopes (RI) were monitored for separation with an RI detector using a lab-made separation LC system. Under the proper separation conditions, the n.c.a ¹⁶⁶Ho was effectively obtained from a large amount of 100 mg dysprosium target within 2 hrs.

• Journal of Life Science
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• v.14 no.5
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• pp.794-799
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• 2004

Cyclodextrin glucanotransferase (CGTase) produced by Bacillus subtilis NAl/pKBl was used for the production of cyclodextrin (CD). The enzyme was purified by ion exchange and gel filtration chromatography. The purified enzyme exhibited its maximum activity in the pH range of 6.0 to 7.0 and temperature range of 60 to $70^{\circ}C$. Immobilization of purified CGTase was carried out with various immobilization matrices. Amberlite IRA-900, a strong basic anion exchange resin, showed the highest immobilization ability (38 units per gram resin). Optimal pH and temperature for enzymatic reaction of the immobilized CGTase were pH 6.0 and 60t. The activity of immobilized CGTase maintained more than a month and could be reused for a month in a continuous enzyme reactor for the production of CD.

• KSBB Journal
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• v.14 no.2
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• pp.248-254
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• 1999

Adverse reactions after injection of diphtheria vaccine are induced by impurities present in crude toxoids that cannot be removed completely by purification of toxoids after formalization. To increase toxoid purity, toxin purification was tried before formalization. Crude toxin was purified with ultrafiltration and ion-exchange chromatography. Purified toxin purity was improved 2.9 times higher than crude toxin, and purity was 2,560 Lf/mg PN. Purified toxin was detoxified with formalin and lysine, and potency test were performed. Toxoid, prepared from toxin treated with formalin and lysine, did not show reversion to toxin and purity was higher than the toxoid purified after formalization. Therefore, we concluded that the use of toxoid vaccine prepared from toxin purified is a useful method of minimize adverse reaction after injection of diphtheria vaccine.