• Journal of Microbiology and Biotechnology
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• v.13 no.6
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• pp.989-992
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• 2003

Recombinant human tissue plasminogen activator deletion mutein (Reteplase) is a clinically promising thrombolytic drug. Reteplase cDNA was subcloned into a bacteria expression system, and the resultant recombinant was biologically characterized. The Reteplase was expressed in Escherichia coli as an inclusion body, and the downstream processes of the Reteplase inclusion body included denaturation, renaturation, and purification. A protein disulfide isomerase (PDI) was used to assist the refolding of Reteplase, and it was found to increase the refolding rate from less than 2％ to more than 20％. The refolded Reteplase was purified through two chromatography steps, including lysine-coupled agarose affinity chromatography and then CM-sepharose cation-exchange chomatography. The purity of r-PA was analyzed by Western bolt analysis, and N-terminal amino acid and amino acid composition analyses confirmed the end-product. Reteplase showed higher thrombolytic potency in an animal thrombus model.

• Journal of the Society of Cosmetic Scientists of Korea
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• v.14 no.1
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• pp.1-15
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• 1988

A new method for liquid chromatography with post column reaction is suggested for the separation and quantification of tertiary amines. A mixture of triethanolamine and N-ethyl diethanolamine was separated by a strong cation exchange column, followed by spectrophtometric detection of the blue colors generated from the reaction of each amine with the Folin-Ciocalteau reagent. The tertiary amines were properly separated when an eluent of pH 9.5 containing 0.5M sodium nitrate was used. Under this condition, calibration curve of triethanolamine in 2-10mg/100ml concentration range was attained. Good results were obtained when cream and shampoo preparations containing known amount of triethanolamine were analysed according to this method. In case the sample did not contain any other interfering reducing substances, the amine was quantitatively determined by the simple reaction of the samples with Folin-Ciocalteau reagent, and the subsequent spectrophotometric measurement.

• Applied Biological Chemistry
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• v.16 no.2
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• pp.53-59
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• 1973

The anthocyanins in Santa rosa plum (widely growing var. in Korea) were extracted with 0.5% methanolic HCl and purified with Amberlite IRC-50 cation exchange resin. The individual pigments were separated by paper chromatography. The two pigments were identified as cyanidin-3-monoglucoside and cyanidin-3-xyloglucoside based on the following evidence: Rf values in various solvents, partical acid hydrolysis, stepwise hydrolysis, sugar moiety, alkaline degradation, and absorption spectra in the visible region. Cyanicin-3-monoglucoside was the abundant pigment of the plum.

• Mycobiology
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• v.41 no.3
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• pp.149-154
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• 2013

An ${\alpha}$-glucosidase inhibitor was developed from Aspergillus oryzae N159-1, which was screened from traditional fermented Korean foods. The intracellular concentration of the inhibitor reached its highest level when the fungus was cultured in tryptic soy broth medium at $27^{\circ}C$ for five days. The inhibitor was purified using a series of purification steps involving ultrafiltration, Sephadex G-25 gel permeation chromatography, strong cation exchange solid phase extraction, reverse-phase high performance liquid chromatography, and size exclusion chromatography. The final yield of the purification was 1.9%. Results of the liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis indicated that the purified ${\alpha}$-glucosidase inhibitor was a tri-peptide, Pro-Phe-Pro, with the molecular weight of 360.1 Da. The IC50 value of the peptide against ${\alpha}$-glucosidase activity was 3.1 mg/mL. Using Lineweaver-Burk plot analysis, the inhibition pattern indicated that the inhibitor acts as a mixed type inhibitor.

• Journal of Microbiology
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• v.35 no.4
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• pp.323-326
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• 1997

Toxin protein from Ustilago maydis virus SH14 isolated in Korea was purified using ethanol precipitation, cation exchange, gel filtration and anion exchange chromatography. The molecular weight of the purified protein was estimated to be 8.3 kDa by SDS-PAGE analysis. The Nterminal sequence of the protein is L-G-I-N-C(K)-R-G-S-S-Q--C(K)-G-L-S-G which is highly homologous with that of P4 toxin, but the amino acid composition and electrophoretic mobility in a native PAGE of the toxin protein were totally different from those of P4 toxin respectively. The SH14 toxin was shown to have immunological cross-reactivity about 50% with P4 toxin when examined by Western hybridization.

• The Korean Journal of Nuclear Medicine
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• v.3 no.1
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• pp.69-72
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• 1969

In 1968 total 94,660 mc of radioactive iodocompound were prepared and distributed to the urers. In order to obtain an effective liver scanning In-113 m colloidal of even particle size from a $^{113}Sn-^{113m}In$ cow, the eluate(pH; 1.5) was examined by a radio paper partition chromatography. It was found that the eluate was composed of two components, ionic form and colloidal form. The ionid form could be eliminated by cation exchange resine and the eluate from the ion exchange resine was of even particle size to give an excellent liver scanning result. Labelling of $^{113m}In$ to human serum albumine was attempted.

• Applied Chemistry for Engineering
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• v.27 no.6
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• pp.633-638
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• 2016

In this study, we used three kinds of commercially available cation, anion, and mixed-ion exchange resins to separate radioactive ions from a polluted water containing Cs, I, and other radioactive ions. The experiment was conducted at a room temperature with a batch method, and a comparative analysis on the decontamination ability of each resin for the removal of Cs and I was performed by using different quantities of resins. The concentration was analyzed using ion chromatography and the ion exchange resin product from company D showed an overall high ion exchange ability. However, for most of the experiments when the amount of ion exchange resin was decreased, the decontamination ability of the resins against mass increased. When the mass of company D's cation exchange resin was small, the ion exchange ability against Cs and I ions were measured as 0.199 and 0.344 meq/g, respectively. When the mixed ion exchange resin was used, the ion exchange ability against I ions was measured as 0.33 meq/g. All in all, company D's ion exchange resins exhibited a relatively higher ion exchange ability particularly against I ions than that of other companies' exchange ions.

• Journal of Animal Science and Technology
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• v.46 no.1
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• pp.77-82
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• 2004

This study was carried out to establish the purification protocol of angiogenin(ANG) from bovine milk. The purification of ANG from bovine milk was performed by using cation chromatography, high-performance liquid chromatography and gel-filtration. We obtained the ANG protein have the molecular weight of about 14 kD by SDS-PAGE analysis. This protein was confirmed as ANG by Nlb-terminal sequence analysis of the first 15 amino acids. Identified amino acids revealed the protein to be identical to that previously reported for bovine ANG.

• Microbiology and Biotechnology Letters
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• v.26 no.5
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• pp.379-386
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• 1998

Deterioration of food is in general caused by the presence of microorganisms and chemical compounds of food itself. There exists antimicrobial compound in the food, however, addition of food antiseptics, additives, or physico-chemical processing is a common practice. The safety of artificial chemical antiseptics became a serious public concern, therefore, new natural antiseptic compounds are in need to be developed. We have isolated a new natural antifungal protein (KBS-B2) from Astragal seed through ammonium sulfate precipitation and column chromatography using FPLC Mono-S and Superose 12HR. The purified protein inhibited growth of Candida albicans, and spore germination of food spoiling fungi such as Aspergillus ochraceus, Penicillium expensum, P. digitatum and Botrytis cineria. Antifungal effect of the KBS-B2 protein could be directly assayed by bioautography overlaying the fungal spores on the electrophoresed acrylamide gel. The comparison of N-terminal amino acid sequences of the KBS-B2 with known antifungal protein revealed that had 50% homology to thaumatin and zeamatin like proteins.

• KSBB Journal
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• v.18 no.2
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• pp.122-126
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• 2003

Multi-cycle chromatographic separation of Iysozyme from egg white was investigated. Multi-cycle chromatography was performed by repeated cycling(one cycle: resin equilibration, sample loading, washing, elution). Two types of cation exchange resins, Cellufine CM C-200 and Bio-rex 70, were used to determine the optimum condition for the separation of Iysozyme by multi-cycle chromatography. The resin was equilibrated in 20 mM Na-phosphate buffer(pH 7.0). Chromatograms of UV absorbance levels of every cycle were compared to confirm the eluting ability of Iysozyme in the two types of gel. Collected samples from eluting regions in every cycle were assayed by 15% SDS-PAGE.