• Journal of Plant Biology
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• v.33 no.4
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• pp.325-332
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• 1990

Light membrane vesicles were isolated from the zucchini hypocotyl by floatation on ficoll density gradients and the proteins were solubilized with Triton X100. Three ATP-hydrolyzing enzymes were partially purified by ion-exchange and gel filtration chromatography and isoelectric focusing. There are plasma membrane-type ATPase whose activity was inhibited by vanadate but not by nitrate, tonoplast-type ATPase which was sensitive to nitrate but insensitive to vanadate and one having a phosphatase activity with a pI value different from that of an acid phosphatase. A fraction was obtained after DEAE-ion-exchange chromatography crossreacting with polyclonal antibodies against Ca2+ -ATPase from human erythrocytes.

• Bulletin of the Korean Chemical Society
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• v.30 no.10
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• pp.2429-2432
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• 2009

• Journal of the Korean Chemical Society
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• v.30 no.2
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• pp.224-230
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• 1986

Dodecyltrimethylammonium bromide (DTAB) was examined as a counter-ion in the separation of aromatic sulfonic acids on alkylmodified silica (ODS) column by reversed-phase ion-pair chromatography. The capacity factor of acids was investigated and separation was attempted. The capacity factor of samples was influenced by the several factors such as a concentration of counter-ion, concentration of methanol, kinds and concentration of electrolyte in mobile phase as well as kinds and position of functional group in samples. Some mixtures of samples were able to be separated under optimum condition.

• Journal of Animal Science and Technology
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• v.47 no.6
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• pp.1025-1032
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• 2005

This study was carried out to separate ovotransferrin in chicken egg white by gel chromatography and heparin affinity chromatography. In gel filtration which was performed with 50mM Phosphate buffer (pH 7.2, 0.15M salt) at a flow rate of 2.0 ml/min, ovotransferrin and ovalbumin were eluted together in fraction number 11-16. In order to separate pure ovotransferrin, fraction No. 12-14 of them which have high concentration of ovotransferrin were concentrated and rechromatographed. However, the ovotransferrin did not separated clearly. In heparin affinity chromatography, the separation was performed with 50mM ethylaminetetraacetic acid (EDTA, pH7.2) and 50mM Phosphate buffer (pH 7.2, 0.15M salt contained) on ferrous and ferric ion saturated column at as same flow rate as gel filtration system's. Ovotransferrin and albumin were eluted together at 10-15min (fraction No.3) and 15-20min (fraction No.4), respectively. However, purified ovotransferrin was eluted at 156-165min and 165-175min (tube No.32-33) with 50 mM phosphate buffer (pH 7.2, 0.15M salt free), respectively. Heparin affinity chromatography with ferric ion saturated column was resulted in the best separation of ovotransferrin rather than separation by gel chromatography and ferrous ion saturated heparin affinity chromatography.

• Analytical Science and Technology
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• v.19 no.1
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• pp.31-38
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• 2006

Micellar electrokinetic capillary chromatography(MECC) and HPLC with ion-pairing mechanism were applied for the separation of the well known environmental wastes from dye industry. These compounds include H-acid, J-acid, ${\gamma}$-acid, orthanilic acid, sulfanilic acid and 2-naphthylamine-1,5-disulfonic acid, and are known to be the diazo components of the azo dye. MECC method was also applied to separate few acid dyes including Acid Orange 7, Acid Orange 5 and Acid Blue 92 and direct dye such as Direct Red 80. Informations about the diazo components of any azo dye could be obtained by comparison of electropherogram of the reduction solution of a given dye with those obtained from standard materials such as H-acid, J-acid, ${\gamma}$-acid, orthanilic acid, sulfanilic acid and 2-naphthylamine-1,5-disulfonic acid. It has been concluded that MECC and HPLC with ion-pairing mechanism could be successfully applied for the analysis of unknown dyes and their diazo components.

• Journal of Korean Society of Occupational and Environmental Hygiene
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• v.7 no.2
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• pp.223-232
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• 1997

The accuracy and precision of a modified method of NIOSH Method 7600 and EPA method 218.6 was determined for analyzing hexavalent chromium, Cr(VI), collected on PVC filter from workplace air. The method was designed to extract from Cr(VI) on PVC filter with a alkali solution, 2% NaOH/3% $Na_2CO_3$, and to analyze it using ion chromatography/visible absorbance detection(IC/VAD). The results and conclusion are as the following. 1. The peak of Cr(VI) was separated sharply on chromatogram and was linearly related with Cr(VI) concentration in sloution. The correlation coefficient was 0.9999 in a calibration curve. The limit of detection was 0.25 $0.25{\mu}g/sample$. 2. The accuracy(% recovery) was 93.3% in a set of sample($9-50{\mu}g$) stored for a day, and 100.1%($10-60{\mu}g$) in another set of samples stored for 2 hours. It is assumed that the difference in recovery by storage time was due to reduction of Cr(VI) to Cr(III). 3. The precision(coefficient of variation, CV) of the method was 0.015 in spiked samples with Cr(VI) standard solution, and 0.010 in spiked samples with plating solution from a chrome electroplating factory. The overall CV in all types of samples was 0.0013. 4. The Cr(VI) was stable in 2% NaOH/3% $Na_2CO_3$ at least for 10 hours. In conclusion, the IC/VAD method is appropriate for determining low-level Cr(VI) in workplace air containing various interferences.

• Korean Journal of Microbiology
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• v.29 no.2
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• pp.92-96
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• 1991

The soluble cytochrome c-551 of photosynthetic bacterium, Rhodopseudomonas gelatinosa ATCC 17013 was purified through a sequene of four step chromatography including CM-cellulose ion-exchange chromatography, DEAE-Sephacel chromatography, Sephacryl s-200 gel permeation chromatography, and HPLC (SP-5PW). The molecular weight of the purified cytochrome c-551 was 14, 600 Da, and this protein shows the absorption peak at 551 nm, 522 nm, and 417 nm as the reduced form, and at 412 nm as the oxidized form. The cytochrome c-551 seems to be a substrate for the terminal oxidase in the electron transport chain.

• Journal of Korean Society of Environmental Engineers
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• v.32 no.4
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• pp.349-356
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• 2010

Ion chromatography (IC) coupled with conductivity detector (CD) is a common system for the determination of perchlorate in water samples. Although the IC method with CD has been widely used for the determination of trace level perchlorate ion in water, sensitivity decreases dramatically as the complexity of the matrices increases. Here we proposed the application of ion chromatography coupled with mass spectrometry (IC-MS/MS) to significantly improve selectivity of perchlorate. The mean recovery of the method was 104.4 ${\pm}$ 5.7% and the relative standard deviation (RSD%) was 1.9 ${\pm}$ 1.3%. The alculated method detection limit (MDL) was 0.0207 ${\pm}$ 0.0099 ${\mu}g/L$. The concentrations of perchlorate were minimum <0.1 ${\mu}g/L$ and maximum 18.3 ${\mu}g/L$ in source water (Namhan, Bukhan and Han River). Hongreung showed higher concentrations ($1^{st}$-14.3 ${\mu}g/L$, $2^{st}$-18.3 ${\mu}g/L$) than the other places. And the concentrations of perchlorate were 0.18~0.34 ${\mu}g/L$ in the samples taken from the six water treatment plants and six intake stations in Seoul.

• Microbiology and Biotechnology Letters
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• v.18 no.6
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• pp.585-590
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• 1990

The cyclodextrin glucanotransferase (CGTase) was purified from the culture broth of Bacillus stearothermophilus by ammonium sulfate precipitation and affinity chromatography. The specific activity of the CGTase increased by about 31-fold from 111.5 U/mg protein to 3445.0 Ulmg protein. The SDSPAGE indicated that the purified CGTase was homogeneous and the molecular weight of the purified CGTase was about 78,000. The optimum pH and temperature was 6.0 and $60^{\circ}C$, respectively. This enzyme was stable from pH 5.5-10.0. The enzyme retained its full activity at the incubation temperature up to $60^{\circ}C$ and calcium ion increased the thermal stability. The isoelectric point was about 4.8.

• Fisheries and Aquatic Sciences
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• v.17 no.2
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• pp.181-187
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• 2014

This study was performed to identify the optimum fractionation method and conditions to obtain exopeptidase-active fractions from octopus hepatopancreas (HP) crude extracts (CEs) using four techniques: solid ammonium sulfate fractionation, polyethylene glycol (PEG) fractionation, anion exchange chromatography, and gel filtration chromatography. The fractions with the highest total activity toward L-leucine-p-nitroanilide (Leu-pNA) were fraction IV from the ammonium sulfate and PEG fractionation, and fraction II in ion exchange and gel filtration chromatography. The total exoprotease activity of these fractions was highest in fraction IV (4,050.20 U) of ammonium sulfate fractionation, followed by fraction II (3,600.28 U) from gel filtration chromatography, fraction IV (2,861.30 U) from PEG fractionation, and fraction II (2,576.28 U) from ion exchange chromatography. These results suggest that ammonium sulfate fractionation using 60-80% ammonium sulfate was the most efficient method for separating the exoprotease active fractions from CEs of octopus HP.