• YAKHAK HOEJI
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• v.25 no.4
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• pp.137-143
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• 1981

In order to confirm the exact antipyretic component in the earthworm, etherial extract of American earthworm(Red Worm) was fractionated into five fractions by using silica gel column chromatography and thin layer chromatography. The fraction including free fatty acids was found to possess artipyretic response and standard arachidonic acid showed marked antipyretic response on typhoid vaccinated rabbits. Arachidonic acid was identified from the free fatty acid fraction of the earthworm by using gas liquid chromatography. Thus it was considered that the antipyretic activity of the free fatty acid may be due to the presence of arachidonic acid. Lipid-free earthworm powder was extracted with phosphate buffer (pH, 8.0, 0.1M) and all the proteins was salted out by ammonium sulfate. The crude precipitate was dialyzed and the impure proteins were eliminated at pH 5.4 and 4.6. The remaining protein solution was fractionated with various concentrations of acetone. The acetone fractions were identified by using S.D.S. polyacrylamide gel electrophoresis and disc gel electrophoresis. The precipitate at 85% acetone concentration and the remaining proteins in the supernatant did not exhibit the antipyretic activity.

• Korean Journal of Agricultural Science
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• v.13 no.2
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• pp.299-310
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• 1986

The ovine squamous cell carcinoma (OSCC)-specific and immunosuppressive properties of OSCC extracts were investigated by using the techniques of lymphocyte blastogenicity, acid dissociation-ultrafiltration and gradient polyacrylamide gel electrophoresis. It was found that OSCC extracts contained two major and one minor protein peaks by Sephadex gel fractionation. Two major peaks bear substantial amount of immunoglobulins, antigen-antibody complex and OSCC-specific fractions, and the minor peak includes immunosuppressive materials. OSCC-specific components were detected at the molecular weights of 10,000 to 100,000 daltons in the major peaks and immunosuppressive materials at the fractions with the molecular weight of 10,000 to 100,000 and < 10,000 daltons in the minor peak. When the fractions were further separated by gradient polyacrylamide gel electrophoresis, the OSCC-specific antigens were found in the slice number 4 to 6 in fraction III, and immunosuppressive materials, in the slice numbers 9 to II in fraction V. The present results were considered to provide a basis for preparation and purification of OSCC-specific and immunosuppressive materials from the crude OSCC extracts.

• Korean Journal of Microbiology
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• v.26 no.3
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• pp.223-229
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• 1988

Bacillus subtilis K-4-3, which produces considerable amount of $\beta$-glucanase was selected among extracellular $\beta$-glucanase-producing bacteria isolated from soil. $\beta$-glucanase was purified by ammonium sulfate fractionation, Sephadex G-100 gel filtration and DEAE-sephacel ion exchange chromatography. The purified enzyme revealed a single band by polyacrylamide gel electrophoresis and SDS-polyacrylamide gel electrophoresis. Its molecular weight was estimated to be 17000 dalton by SDS-polyacrylamide gel electrophoresis. The optimum pH and temperature of the purified $\beta$-glucanase were 7.0 and $50^{\circ}C$, respectively. The enzyme was strongly inhibited by 1.0mM of $Fe^{3+}$, and activated by 1.0mm of $Li^{}47+$. The absence of glucose after thin layer chromatography of reaction products revealed that the purified enzyme contains no cellobiase or laminarinbiase activity. The loberation of ki, tri-and tetra-saccharide as reaction products can be explained by endoaction of the enzyme.

• Korean Journal of Food Science and Technology
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• v.16 no.3
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• pp.322-328
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• 1984

These experiments were conducted to purify the glucoamylase produced by Rhizopus oryzae. Two forms of glucoamylase (GI and GII) from Phizopus oryzae were purified by $(NH_2)_2SO_4$ fractionation, acetone fractionation and successive column chromatography on DEAE-cellulose and CM-cellulose. The specific activities of GI and GII toward soluble starch were 157.6 U/㎎. protein (37.5 fold of crude extract), and 164.7 U/㎎. protein (39.2 fold of curde extract), respectively, and the yields of them were 4.3% and 3.8%, respectively. The two purified enzymes have shown a single band by polyacrylamide disc gel electrophoresis and SDS-polyacrylamide gel electrophoresis. The protein bands of their electrophoresis gel were revealed to have glucoamylase activity by iodine staining and were proved to be glycoprotein by periodic acid Schiff's staining.

• Journal of Microbiology and Biotechnology
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• v.1 no.2
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• pp.90-95
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• 1991

A ${\alpha}-galactosidase{\;}({\alpha}-D-galactoside$ galactohydrolase; EC 3.2.1.22) was purified from the culture filtrate of Penicillium purpurogenum by DEAE-cellulose column chromatography, gel filtration of Bio gel p-l00, and subsequent SP-Sephadex C-25 chromatography. The final preparation thus obtained showed a single band on polyacrylamide disc-gel and SDS-polyacrylamide gel electrophoresis. The molecular weight and isoelectric point were determined to be 63,000 and pH 4.0 by SDS-polyacrylamide gel electrophoresis and isoelectric focusing, respectively. The galactosidase exhibited maximum activity at pH 4.5 and $55^{\circ}C$, and was stable between pH 2 and 5, and also stable up to $40^{\circ}C$. The enzyme activity was not affected considerably by treatment with other metal compounds except mercuric chloride and silver nitrate. Copra galactomannan was finally hydrolyzed to galactose, mannose and mannobiose through the sequential actions of the purified galactosidase and mannanase from the same strain. The enzyme hydrolyzed melibiose and raffinose, but not lactose.

• Korean Journal of Food Science and Technology
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• v.14 no.1
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• pp.1-5
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• 1982

An invertase from Korean ginseng (Panax ginseng C. A. Mayer) was purified by means of DEAE-cellulose column chromatography and gel-filtration through Sephadex G-75. The homogeneity of the purified invertase was proved by polyacrylamide gel disc electrophoresis. The enzyme was separated into two subunits by SDS-polyacrylamide gel electrophoresis, showing its molecular weights as 48,000. The enzyme preparation showed a characteristic protein UV-spectra.

• Journal of the Speleological Society of Korea
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• no.76
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• pp.49-55
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• 2006

The submicron $YBa_2Cu_3O_x$ powder was prepared by the sol-gel method. The particle size is distributed from 0.2 to 1.0 ${\mu}m$, which benefits to eliminate the micro-cracks formed in the $YBa_2Cu_3O_x$ films deposited by electrophoresis. The powder was single phase of $YBa_2Cu_3O_x$ examined by X-ray diffraction. In the sol-gel process the citrate gel was formed from citric acid and nitrate solution of $Y_2O_3$, $Ba(NO_3)_2$ and CuO. When pH values were adjusted to 6.4-6.7, $Ba(NO_3)_2$ could be dissolved in the citrate solution completely. Appropriate evaporative temperature of the sol-gel formation is discussed. Acetone is used as electrophoreticsolution, in which some water and iodine (0.2 g/1) and polyethylene glycol (2 vol. %) are added. The concentrations of $YBa_2Cu_3O_x$ powders is 20g/l. The thickness of deposited film could be more than 50 ${\mu}m$ in 3 minutes of depositing time. The most EPD films could be 90K zero resistance and the Jc values were over 1000A/cm2 (0 H, 77 K).

• Bulletin of the Korean Chemical Society
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• v.35 no.4
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• pp.1082-1086
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• 2014

A multi-channel microchip electrophoresis (MCME) method with parallel laser-induced fluorescence (LIF) detection was developed for rapid screening of H1N1 virus. The hemagglutinin (HA) and nucleocapsid protein (NP) gene of H1N1 virus were amplified using polymerase chain reaction (PCR). The amplified PCR products of the H1N1 virus DNA (HA, 116 bp and NP, 195 bp) were simultaneously detected within 25 s in three parallel channels using an expanded laser beam and a charge-coupled device camera. The parallel separations were demonstrated using a sieving gel matrix of 0.3% poly(ethylene oxide) ($M_r$ = 8,000,000) in $1{\times}$ TBE buffer (pH 8.4) with a programmed step electric field strength (PSEFS). The method was ~20 times faster than conventional slab gel electrophoresis, without any loss of resolving power or reproducibility. The proposed MCME/PSEFS assay technique provides a simple and accurate method for fast high-throughput screening of infectious virus DNA molecules under 400 bp.

• Proceedings of the Korean Society of Applied Pharmacology
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• 1993.04a
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• pp.45-45
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• 1993

괄루근으로부터 분리된 다당류에 대하여 continuous gel electrophoresis, SDS-Polyacrylamide gel eletrophoresis, ion exchange column chromatography, Hydroxyapatite column chromatography 및 Gel filtration등의 방법을 이용하여 다음과 같은 결과를 얻었다. 1) 황산암모늄 분별침전법에 의한 렉틴의 정제도는 초추출물의 4.85배이며 DEAE Sephadex A-50 column chromatography법에 의한 정제도는 24.17배로 나타났고, 마지막 정제단계인 Sephacryl S-200 gel filtration에 의한 정제도는 47.34배로 나타났다. 2) 정제된 렉틴의 분자량은 60,000da1ton으로 나타났다. 3) 사람의 혈액형에 따른 응집효과는 90-100％로 특이성은 없었다.

• KSBB Journal
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• v.20 no.2 s.91
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• pp.71-75
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• 2005

Alignment of 2D-gel images of biological samples can visualize the difference of expression profiles and also inform us candidates of protein spots to be further analyzed. However, comparison of two proteome images between the case and control does not always successfully identify differentially expressed proteins because of sample-to-sample variation, poor reproducibility of 2D-gel electrophoresis and inconsistent electrophoresis conditions. Multiple alignment of 2D-gel image must be preceded before visualizing the difference of expression profiles or clustering proteome images. Thus, a software for the alignment of multiple 2D-Gel images and their clustering was developed by applying various algorithms and statistical methods. Microsoft Visual C++ was used to implement the algorithms in this work. Multiresoultion-multilevel algorithm was found out to be suitable for fast alignment and for largely distorted images. Clustering of 10 different proteome images of Fetal Alcohol Syndrome, was carried out by implementing a k-means algorithm and it gave a phylogenetic tree of proteomic distance map of the samples. However, the phylogenetic tree does not discriminate the case and control. The whole image clustering shows that the proteomic distance is more dependent to age and sex.