• Analytical Science and Technology
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• v.6 no.5
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• pp.471-477
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• 1993

The novel macrocylic ligand {(4, 5):(13, 14)-dibenzo-6, 9, 12-trioxa-3, 15, 21, -triazabicyclo [15. 3. 1]heneicosa-(1, 17, 19)(18, 20, 21) triene: HDBPDA} was synthesized, and protonable constants of the ligand and the complex stability constants with alkali metals alkaline earth metals were determined. We evaluated the resolution factor(${\Delta}$) from equation that inducing from stability constants(pK). Also, this ligand was grafted on chloromethylated styrene-divinyl benzene(Merrifield resin) for HDBPDA, ion exchanger. Alkali and alkaline earth metal ions were separated using water by the column chromatography with this ion exchanger. Selectivity(${\alpha}$) and resolution(Rs) of alkali and alkaline earth metal ions were measured from the elution curves chromatogram. The selectivity and resolution values of the various ions calculated from the elution curves were compared with those abtained from pK values. The results were in a good agreement between tow methods. Ion exchange capacity of the resin were determined using the alkali and alkaline earth metal ions and pH dependence of capacity was also discussed.

• Journal of the Korean Chemical Society
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• v.34 no.1
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• pp.69-75
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• 1990

An ion-association chromatography was applied for the separation and determination of individual rare earth elements (REE) contained in mineral monazite. Prior to the determination, the group separation of REE was achieved by a cation exchange column of Dowex 5OW-X8 resin. The quantitative recovery of REE by the resin column, free from coexisting elements in monazite, was confirmed with radioactive tracers as well as with ICP-MS. Individual REE at ppm level was separated on reversed-phase column ($\mu$-Bondapak $C_{18}$) using gradient elution from 0.05 to 0.3 M $\alpha$-hydroxyisobutyric acid at pH 4.6. The individual REE was detected at 546 nm following post-column reaction with PAR (4-(2-pyridylazo)-resorcinol monosodium salt).

• Bulletin of the Korean Chemical Society
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• v.28 no.3
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• pp.451-456
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• 2007

Tetraazamacrocyclic ion exchangers tethered to Merrifield peptide resin (DTDM, TTTM) were prepared and the ion exchange capacity of these was characterized. The isotope separation of lithium was determined using breakthrough method of column chromatography. The isotope separation coefficient was strongly dependent on the ligand structure by Glueckauf's theory. We found that the isotope separation coefficients were increased as the values of distribution coefficients were increased. In this experiment the lighter isotope, 6Li was enriched in the resin phase, while the heavier isotope, 7Li in the solution phase. The ion radius of lighter isotope, 6Li was shorter than the heavier isotope, 7Li. The hydration number of lithium ion with the same charge became small as mass number was decreased. Because 6Li was more strongly retained in the resin than 7Li, the isotopes of lithium were separated with subsequent enrichment in the resin phase.

• Journal of the Korea Academia-Industrial cooperation Society
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• v.12 no.10
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• pp.4696-4703
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• 2011

Tetraazamacrocyclic ion-exchangers, 1,4,8,11-tetraazacyclotetradecane bonded Merrifield peptide resin(TDM), 1,4,8,12-tetraazacyclopentadecane bonded Merrifield peptide resin(TPM) were prepared, and the ion-exchange capacity of these TDM and TPM were characterized. The distribution coefficients in various conc. of NH4Cl for magnesium with ion exchangers were determined by using the batch method. We found the isotope separation factors on new prepared tetraazamacrocyclic ion-exchangers bonded Merrifield peptide resin(TDM, TPM). The isotope separation of magnesium was determined by using of breakthrough method of column chromatography.

• 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.

• Archives of Pharmacal Research
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• v.21 no.3
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• pp.291-297
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• 1998

Cop protein has been overexpressed in Escherichia coli using a T7 RNA polymerase system. Purification to apparent homogeneity was achieved by the sequential chromatography on ion exchange, affinity chromatography, and reverse phase high performance liquid chromatography system. The molecular weight of the purified Cop was estimated as 6.1 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). But the molecular mass of the native state Cop was shown to be 19 kDa by an analytical high performance size exclusion chromatography, suggesting a trimer-like structure in 50 mM Tris-HCI buffer (pH 7.5) containing 100 mM NaCl. Cop protein Was calculated to contain $39.1% {\alpha}-helix, 16.8% {\beta}-sheet$, 17.4% turn, and 26.8% random structure. The DNA binding property of Cop protein expressed in E. coli Was preserved during the expression and purification process. The isoelectric point of Cop was determined to be 9.0. The results of amino acid composition analysis and N-terminal amino acid sequencing of Cop showed that it has the same amino acid composition and N-terminal amino acid sequence as those deduced from its DNA sequence analysis, except for the partial removal of N-terminal methionine residue by methionyl-aminopeptidase in E. coli.

• BMB Reports
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• v.29 no.5
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• pp.455-461
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• 1996

A serine proteinase was purified from Acanthamoeba culbertsoni by 41~80% ammonium sulfate fractionation, ion exchange chromatography, affinity chromatography and gel filtration chromatography. The molecular weight of the purified enzyme was estimated to be 108.0 kDa by gel filtration chromatography and 54.0 kDa by SDS-PAGE. Therefore, the purified enzyme seemed to be a dimer. Isoelectric point was 4.5. The enzyme activity was highly inhibited by the serine proteinase inhibitors diisopropyl fluorophosphate (OFP) and phenylmethyl sulfonylfluoride (PMSF). It had a narrow pH optimum of 6.5~7.5 with a maximum at pH 7.0. These data suggested that the purified enzyme was a neutral serine proteinase. Optimal temperature was $37^{\circ}C$. It was stable for at least 16 h at $4^{\circ}C$ and $37^{\circ}C$, but it was rapidly inactivated at $65^{\circ}C$ The activity of the purified enzyme was not influenced significantly by $Mg^{2+}$, $Mn^{2+}$, $Zn^{2+}$ or $Ca^{2+}$. However, the enzyme activity was highly inhibited by $Hg^{2+}$ The enzyme degraded type I collagen and fibronectin, but not BSA, hemoglobin, lysozyme, immunoglobulin A or immunoglobulin G.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.38 no.2
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• pp.83-88
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• 2005

Protease inhibitors were purified from the eggs of Alaska pollock (Theragra chalcogramma) using the following purification steps: ammonium sulfate precipitation, ion exchange, gel permeation, and high performance liquid chromatographies (HPLC). The protease inhibitor from the heated eggs of Alaska pollock was not as well purified. In addition, the heated eggs showed lower specific inhibitory activity than the unheated eggs. The purification yields after ammonium sulfate precipitation, ion exchange, and gel permeation chromatographies were 22.7$\%,\;15.3\%$,and $4.4\%$, respectively. There were two kinds of protease inhibitors on the gel permeation chromatography pattern Their molecular weights were estimated to be 66,700 and 16,000 Da, respectively. Both were classified as a cysteine protease inhibitor because of the existence of inhibiting papain, which is one of cysteine proteases.

• Journal of Marine Bioscience and Biotechnology
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• v.2 no.3
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• pp.142-148
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• 2007

An agar-degrading marine bacterium, strain AS-3 was isolated from the seawater. The strain AS-3 was identified as Algibacter lectus AS-3 by 16S rDNA sequence. The optimum medium for agarase activity of the isolated strain was determined to be marine medium, marine broth 2216 containing 0.1% agar as carbon source. An extracellular agarase was purified 6.9-fold from the culture supernatant by ammonium sulfate precipitation, ion exchange chromatography and gel filtration methods. The optimum pH and temperature for this enzyme were 7.0 and $40-50^{\circ}C$, respectively. Antioxidative activity of the strain AS-3 was 62.4% in the supernatant cultured for 12 h.