• Applied Biological Chemistry
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• v.41 no.6
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• pp.410-413
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• 1998

The major protein (GMP) from the roots of Panax ginseng C. A. Meyer was purified, using gel filtration and ion exchange chromatography followed by reversed-phase and ion exchange FPLC. Staining analysis indicated that the protein has a carbohydrate moiety, which was also shown by band shift experiments using various glycosidases. Electrophoretic and gel permeation studies showed that GMP has an apparent molecular weight of 63 kDa composed of possibly two subunits of 25 kDa containing carbohydrate moiety. GMP showed an anticomplementary activity on the hemolysis of red blood cells, which is a screening tool for inflammation mediator search.

• 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.

• Korean Journal of Food Science and Technology
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• v.24 no.6
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• pp.616-618
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• 1992

The study was attempted to isolate taurine from the oyster shucking juice known as one of the by-products of oyster processing using ion exchange column chromatography. Three hundred grams of the oyster shucking juice were loaded onto a column packed with 300 ml of the Dowex 50W $H^+$ form. And taurine-rich fractions were further purified in columns packed with 150 ml of Dowex 2 OH form and the 150 ml of Amberite IRA-410 OH form consecutively. The purity and the yield of taurine recovered from the oyster shucking juice by this method were 94.7% and 84.8%, respectively.

• Journal of environmental and Sanitary engineering
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• v.4 no.1 s.6
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• pp.7-15
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• 1989

According to the increase of population and development of industrialization air and water pollution problems are still keeping going to great nuisance to human activities. Specially man should drink 2l clean water to maintain our health every day, but we afraid of drink the city tap water because of the contaminants like heavy metals, bacteria trihalomethane, etc. In the analysis of the anions in potable water, we usually adapt the Standard methods for the Examination of Water and Wastewater. But this method is tedious and time consuming, so the Ion Chromatography method is now used in research of water quality. Author worked with Ion Chromatography in measuring the anions in drinking water by attaching conductivity dector to normal High Performance Liquid Chromatograph. Low-capacity ion-exchange coulmn and dilute eluents, 0.00M phthalic aic was used in this study. The concentration of chloride ion was 1.55 ppm$\~$3 8.81ppm, nitrate ion was 5.45 ppm$\~$18.27ppm, and sulfate ion was 19.64 ppm$\~$28.86 ppm. The phosphate ion was detected only in Apt. tap water as 167.99 ppm whose amount was supposed to be used as a water pipe cleaner.

• Journal of Life Science
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• v.11 no.6
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• pp.561-567
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• 2001

To isolate and purify fibrinolytic active substance from Sarcodon aspratus(N $H_4$)$_2$S $O_4$ precipitation, DE52 anion exchange column chromatography, Sephacryl-S 200gel filtration chromatography and Mono S cation FPLC were carried out and the characterizations of the purified enzyme were investigated. The bound active fraction on DE52 anion exchange column chromatography were eluted with 0.2 M NaCI and the fibrionlytic enzyme was purified after following Sephacryl-S200 gel fitration chromatography and Mono S cation EPLC. The specific activity of purified enzyme was 55.2 U/mg protein and increased 11.3 fold comparing crude extract and the yield was 49.5%. 12% SDS-PAGE electrophoresis and gel filtration chromatography revealed that Sarcodon aspratus fibrionloytic enzyme was highly purified and had 29.300 Da molecular weight. Enzyme activity of the purified fibrinolytic enzyme from Sarcodon aspratus was increased on higher pH and was stable until pH 10.5. On temperature dependent stability, the enzyme activity was decrease sharply but remained 25% relative activity on 8$0^{\circ}C$. This enzyme activity was inhibited by heavy metal ion, C $U^{2+}$ and $Co^{3+}$ with 68% and 38%, respectively. And also, the enzyme activity was inhibited with $Ca^{2+}$ chelator EDTA and serine protease inhibitor PMSF. These results from this study suggested that the fibrinolycit enzyme from Sarcodon aspratus is a serine protease and the enzyme activity was increased by $Ca^{2+}$ or $Mg^{2+}$ ion.n.ion.n.

• FOCUS: LIFE SCIENCE
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• no.1
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• pp.5.1-5.3
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• 2024

The document discusses the regeneration of Partisil/Partisphere ion-exchange columns in chromatography. It mentions that column efficiency can diminish with use due to the accumulation of sample and/or mobile phase impurities at the head of the column. This can lead to a change in back pressure, lower column efficiency, and sometimes a change in selectivity. The document outlines a procedure that may restore column performance. The document also provides everyday practices to enhance the lifetime of a column. These include using only high-purity HPLC solvents and buffers, using freshly prepared mobile phases and buffers, filtering mobile phases to remove particulates, using appropriate sample clean-up procedures, using a guard column or pre-column filter, and working within the pressure and flow rate limitations of the column. For the regeneration of Partisil/Partisphere SAX, SCX, WAX, and WCX columns, the document suggests passing 20 column volumes of various mobile phases through the column. These include a buffer wash, distilled water, an acid wash, a chelating wash, a methanol wash, and a buffer for separation. The document emphasizes that not all of these wash steps are required for every column clean-up and that some chromatographers require only a combination of certain steps.

• Microbiology and Biotechnology Letters
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• v.13 no.2
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• pp.157-162
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• 1985

The cell cultures and crude extracts of Bacillus sphaericus 1593 K-5 and its mutant Spo-Dl216 were respectively bioassayed against Culex pipiens var. pollens mosquito larvae. The B. sphaeriucs 1593 K-5 showed toxic activity against the larvae. LC$_{50}$ values (cells/$m\ell$) was 2.6$\times$10$^2$. Also the LC$_{50}$ ($\mu\textrm{g}$ Protein/$m\ell$) of the crude extract was 10.26. However, B. sphaericus Spo-Dl216 didn't show toxic activity against the larvae. The soluble cytoplasmic toxin in broken B. sphaeriucs 1593k-5 cells was partially purified by gel permeation chromatography and ion exchange chromatography. Among the fractions of the gel permeation chromatography only a single fraction was found to be toxic. LC$_{50}$ values ($\mu\textrm{g}$ protein/$m\ell$) of the active fraction was 0.182. The active fraction of the gel permeation was subjected to ion exchange chromatography. Only a single fraction showed toxic activity and its LC$_{50}$ values ($\mu\textrm{g}$ protein/$m\ell$) was 0.02..02.

• The Korean Journal of Food And Nutrition
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• v.6 no.4
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• pp.307-313
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• 1993

Bacillus cereus $\beta$-amylase was purified by Sephadex G-100 gel filtration, CM Sephadex C-50 ion exchange chromatography and CM Sephadex C-50 ion exchange rechromatography The purified enzyme showed 871 unit/mg of specific activity. The purified enzyme was identified as homogenious by disc PAGE, SDS-PAGE and analysis of reaction product. The purified enzyme showed optimum pH 7.0. optimum temperature 5$0^{\circ}C$, and was stable at 0~5$0^{\circ}C$ and at pH range of 6~10.

• 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 Plant Biotechnology
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• v.31 no.4
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• pp.319-323
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• 2004

Soluble latex protein fraction excreted from Euporbia lathyris laticifer was resolved by 10% SDS-polyacrylamide gel electrophoresis to identify distinctively displayed latex major protein bands including ELp65, ELp55, ELp43, ELp32 and ELp23. Among them, ELp65 was purified by ammonium sulfate precipitation, gel permeation chromatography and ion exchange chromatography. Its N-terminal amino acid sequencing revealed its homology to the leading region of mature peptide of tomato p69a subtilisin-like protease, suggesting a certain role involved in plant defense system. In the analysis of Southern blot hybridization using PCR-amplified tomato p69a probe DNA, E. lathyris genome was suggested to have a gene family consisting of 3-5 gene members putatively encoding subtilisin-like proteases.