• Proceedings of the Korean Society of Plant Pathology Conference
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• 1999.10a
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• pp.70.1-70
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• 1999

• Proceedings of the Korean Society of Applied Pharmacology
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• 1998.11a
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• pp.52-55
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• 1998

During a survey of new antitumor substances from higher plants, we have found that the crude extract of Simaba cedron Planchon (Simaroubaceae) showed cytotoxic activity (IC$\sub$50/ 0.7 $\mu\textrm{g}$/mL) against P388 leukemia cells. Activity-guided chromatographic purification using P388 cells led to the isolation of five novel quassinoids, cedronolactones A-E (1-5) and nine known quassinoids, simalikalactone D (6), chaparrinon (7), chaparrin (8), glaucarubolone (9), glaucarubol (10), samaderine Z (11), guanepolide (12), ailanquassin A (13), and polyandrol (14). In this seminar, the structural elucidation of 1-5 and the cytotoxic activity of the isolated compounds are discussed.

• Journal of environmental and Sanitary engineering
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• v.14 no.2
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• pp.32-39
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• 1999

The following is experimental result of selecting soil bacteria showing toxicity against Root-knot nematode (Meloidogyne hapla). Out of 286 strains isolated from soil, one(NC67) showing toxicity against M.hapla is selected The selected strain(NC67) is identified of B. thuringiensis subsp. indiana. It proved out that the toxic maerial against M. hapla produce by NC67 strain is an exotoxin. The result of examining the existence of the extercellular toxicity product by the toxic strain(NC67) by usign activated carbon column chromatography, Dowex 50W column chromatography and TLC of silical gel etc. proved out that it is a single material.

• YAKHAK HOEJI
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• v.38 no.6
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• pp.687-695
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• 1994

Lectin from mistletoe(Viscum coloratum) fermented by Lactobacillus plantarum for 1,2,3 days were obtained by salt fractionation, gel filtration, anion exchange chromatography and SDS-PAGE, and compared with the lectin from unfermented mistletoe. The new lectin of molecular weight of about 18,500D from fermented mistletoe was identified.

• Journal of the Korean Applied Science and Technology
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• v.14 no.3
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• pp.97-101
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• 1997

An intracellular, soluble 1,4-benzoquinone reductase was purified from Baker's Yeast by ammonium sulfate precipitation, DEAE-Sephacel anion exchange chromatography, and Sephacryl S-200 gel filtration chromatography. 1,4-Benzoquinone reductase was achieved 123.8 fold purification from crude homogenate with a yield of 11.1%.

• Proceedings of the PSK Conference
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• 2003.04a
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• pp.316.2-317
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• 2003

Immunoglobulin Y (IgY) obtained from chicken as the immunization host brings several advantages to antibody production, such as improved yield, lower cost, longer stability, and higher specificity than mammalian immunoglobulin. In the present study, we attempted to purify Maackia fauriei lectin using antilectin IgY-affinity chromatography in order to produce a good yield and to reduce the purification time. (omitted)

• Journal of the Korean Chemical Society
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• v.28 no.6
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• pp.393-398
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• 1984

Porphyrin-rich materials were obtained from some crude asphalts by gel permeation chromatography and silica gel chromatography. After extraction of each chromatographic fractions through alumina with pyridine, more concentrated metalloporphyrins were obtained. Demetallation of metalloporphyrins was possible without destroying porphyrin ring to provide different type of metal free porphyrins.

• Food Science of Animal Resources
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• v.29 no.2
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• pp.157-163
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• 2009

This study was conducted for the isolation, purification, and characterization of a protease from Korean pear, to see its proteolytic activity on chicken actomyosin and to find the optimum pH and temperature of activity on chicken actomyosin. The protease was isolated from crude extract of Korean pear by ammonium sulfate precipitation. Further purification was done by DEAE-Sepharose ion-exchange chromatography, Mono-Q and Mini-Q column chromatography. The purified enzyme gave a single protein band on SDS polyacrylamide gel electrophoresis and the molecular weight was found to be 38 kDa. The specific activity of purified enzyme was 34,907 unit/mg with 25 fold purification and the yield was 2%. The purified enzyme incubated with chicken actomyosin showed high activity. The optimum pH and temperature for enzyme activity on chicken actomyosin were 6.5 and $70^{\circ}C$, respectively. A protease was purified from Korean pear for the first time and characterized. It was found to be promising for meat tenderization.

• Proceedings of the Korean Society of Life Science Conference
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• 2008.10a
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• pp.51.2-51.2
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• 2008

• YAKHAK HOEJI
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• v.49 no.1
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• pp.6-10
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• 2005

Immunoglobulin Y (IgY) obtained from chicken as the immunization host brings several advantages to antibody production, such as improved yield, lower cost, longer stability and higher specificity than mammalian immunoglobulin. In the present study, we attempted to produce IgY against a sialic acid-binding lectin, Maackia fauriei agglutinin (MFA), from egg yolk of white Leghorn hens. For the isolation of IgY from egg yolk, we applied a water dilution method. The weekly yield of IgY was determined by enzyme-linked immunosorbent assay, with a final yield of anti-MFA IgY from total IgY of approximately $1\%$. The yielded IgY were used to prepare IgY-affinity column conjugated with CNBr-activated Sepharose 4B, which resulted in the lectin being successfully purified in a single step from Maackia fauriei. This purified lectin exhibited the same hemagglutination activity as lectin purified using conventional purification methods.