• BMB Reports
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• 제29권2호
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• pp.116-121
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• 1996

In earlier studies, the genes encoding Escherichia coli thioredoxin and Corynebacterium nephridii thioredoxin C-3 were fused via a common restriction site in the nucleotide sequence coding for the active site of the proteins to generate two chimeric thioredoxins, designated E-C3 (N to C-terminal) and C3-E. The hybrid thioredoxins were overexpressed in E. coli from the cloned chimeric thioredoxin genes by a T7 promoter/polymerase system. To investigate the structure-function relationship of thioredoxin, we purified the E-C3 hybrid thioredoxin through ammonium sulfate fractionation, DEAE-cellulose chromatography, and Sephadex G-50 gel filtration. Its purity was examined on SDS-polyacrylamide gel electrophoresis and the molecular weight of the purified E-C3 hybrid thioredoxin was estimated to be 12,000. On native polyacrylamide gels, the purified E-C3 hybrid thioredoxin shows a much lower mobility than E. coli thioredoxin. E-C3 hybrid thioredoxin exhibits a 40-fold lower catalytic efficiency with E. coli thioredoxin reductase than E. coli thioredoxin. It was shown to catalyze the reduction of insulin disulfide by dithiothreitol. The purified E-C3 hybrid thioredoxin was also characterized in other aspects.

• 한국미생물·생명공학회지
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• 제20권1호
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• pp.25-33
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• 1992

Serratia marcescens ATCC 25419를 질소원이 풍부한 BHI 배지에서 황산 암모늄 분별 침전을 시킨 후 DAEA-Sephacel chromatography, Phenyl-Sepharose hydrophobic chromatography, Sephacryl S-400 gel filtration, native gel elution을 거쳐 ALS isozyme Rf 0.83을 분리하였다. 분리한 ALS isozyme Rf 0.83의 native 형태는 gel filtration을 이용하여 분자량을 측정한 결과, 531,400이었고, SDS-PAGE를 수행한 결과 55,000의 large subunit와 38,900의 small subunit로 구성된 multimer임을 알 수 있었다.

• 한국산학기술학회논문지
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• 제7권3호
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• pp.471-475
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• 2006

랩온어칩(Lab-on-a-chip) 등 미세구조를 갖는 다양한 장치들의 대량 생산이 가능한 사출성형공정 내에서의 미세 흐름 거동의 이해는 매우 중요하다. 본 논문에서는 마이크로 채널 구조 내에서의 사출성형 흐름에 관하여 연구하였다. 흐름 현상을 관찰하기 위하여 투명한 PMMA를 사용하여 가시화 금형(visual mold)을 제작하였다. 실험 대상 물질로는 고분자 용액인 PEO (poly (ethylene oxide)) 와 PA (polyacrylamide) 용액을 선정하였는데, 이는 고분자 용융체의 특징인 높은 점성과 탄성을 갖도록 설계한 것이다. 시간에 따른 흐름현상과 주 채널과 마이크로 채널과의 경쟁적인 흐름 현상을 관찰하였다. 이로부터 마이크로 사출성형 흐름에서 나타나는 마이크로 채널 내의 충전길이에 대한 해석이 가능하였다.

• 한국미생물·생명공학회지
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• 제13권1호
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• pp.87-91
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• 1985

Hpa I endonuclease를 순수 정제하였다. 150g (wet weight)의 Haemophilus parainfluenzae로 부터 얻은 crude extract를 ammonium sulfate fractionation을 거친후 Heparin agarose, SP-sephadex, DEAE-sephadex, phosphocellulose 등 chromatography를 거쳐 최종적으로 0.2mg의 효소를 얻었다. Specific activity는 $2.2{\times}10^6units/mg$이었다. 얻어진 Hpa I endonuclease는 SDS-polyacrylamide gel에서 한개의 band를 보였고, 그 효소활성은 50mM NaCl과 pH 7.0과 7.5사이에서 가장 높았다.

• 기술사
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• 제18권2호
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• pp.16-22
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• 1985

This study was carried out to evaluate the quality of soybean sprouts grown under three different sources of light. The soybean was germinated under light through blue (251 ux), red (751 ux) and white (50 to 200 lux) polyethylene films at 25$^{\circ}C$ for 10hr./day. Vitamin C, chlorophyll, cellulose and total protein contents were determined and texture was evaluated by tasting soybean sprouts soup. protein pattern in the soybean sprouts were investigated using polyacrylamide gel electrophoresis. Vitamin C, chlorophyll and cellulose contents were increased by white light intensity. The texture of the sprouts grown under white light (50 lux, 100 lux) was better than darkness, but fought under 200 lux. Vitamin C contents of soybean sprouts grown under various sources of light (in order of light : blue > white > red) were higher than theses of ones grown in the darkness. Biosynthesis of chlorophyll was not correlated to Vitamin C content. Total protein contents of cotyledon was not changed significantly under light irradiation. But the soybean sprouts grown under different quality of light, hypocotyl was higher than those grown darkness. (37% and 20% higher for blue light and white light) Densitometric tracing of disc polyacrylamide gel electrophoretic patterns showed that protein of hypocotyl under white light had more high molecular weight protein.

• Applied Biological Chemistry
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• 제37권4호
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• pp.243-247
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• 1994

한국산 대추로부터 조직의 연화에 작용하는 endo-polygalacturonase를 gel filtration과 이온교환크로마토그라피에 의하여 단일 단백질로 정제할 수 있었고, 수율은 약 6% 정도였다. 정제된 이 효소는 sodium dodecyl sulfate-polyacrylamide gel electrophoresis에 의하여 분자량이 약 19,000정도의 monomer로 확인되었고, 결정구조는 육각판상 모양을 나타내었다.

• 한국농공학회논문집
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• 제56권3호
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• pp.47-53
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• 2014

We investigated the effect of straw mat cover and soil amendments on the reduction of runoff, non-point source pollution load and yield of a Chinese cabbage from alpine fields. Two plots on sandy loam soil were prepared. Experimental treatments were control and rice straw mat cover (3,300 kg/ha)+Polyacrylamide (PAM) (5 kg/ha)+Gypsum (1 ton/ha) (SPG). A variety of Chinese cabbage was cultivated and runoff was monitored during a growing season in 2012. Monitoring was conducted to seven times. Runoff rate of SPG plot was lower than those of control plot. The reduction rate of runoff from SPG plot was 29.4 % compared to control plot. The reduction rate of suspended solids (SS), total nitrogen (TN) and total phosphorus (TP) load of SPG plot was 86.5 %, 34.7 % and 39.1 %, respectively. Yield of a Chinese cabbage from SPG plot (39,646 kg/ha) was greater than that of control plots (28,482 kg/ha). It was concluded that the use of SPG on soil surface could not only reduce the NPS pollution loads in receiving waters but also help increase the crop yield.

• 한국미생물·생명공학회지
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• 제23권6호
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• pp.695-701
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• 1995

An alkaline lipase producing bacteria was isolated from soil and identified as Serratia liquefaciens AL-11. from the results of analysis of its morphological, biochemical and physiological properties. This strain showed the highest productivity of alkaline lipase when grown at pH 9.0 and 30$\circ$C for 42 hours in the medium of 1% peptone, 0.5% tryptone, 0.9% yeast extract, 1% starch, 1% tween 80, 0.05% CaCl$_{2}$ and 0.05% NaCl. The enzyme was purified by ammonium sulfate treatment, Sephadex G-100 gel filtration and DEAE-Sephadex A-50 column chromatography. The specific activity of the purified enzyme was 27 unit/mg protein and the yield of enzyme activity was 61.3%. The homogeneity of the purified enzyme was verified by polyacrylamide gel disc electrophoresis. Molecular weight of the purified enzyme was estimated about 53,000 by sodium dodecyl sulfate- polyacrylamide gel electrophoresis. This enzyme is composed of 17 amino acids of which glycine, proline and glutamic acid were three miajor acids.

• Geomechanics and Engineering
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• 제13권2호
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• pp.319-331
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• 2017

This vacuum preloading combined with polyacrylamide (PAM) flocculation was proposed to separating solid-liquid in waste slurry and to improving bearing capacity of soft soil ground. By using waste slurry taken from drilled shaft construction site in Shanghai, China, a series of settling column tests with four typical flocculants and one normal for waste slurry were carried out for comparative analysis. The optimal amounts for each flocculant were obtained from the column tests. Then, model tests on vacuum preloading with anionic polyacrylamide (APAM) flocculation and without flocculants were carried out. The out of water and the settlement of slurry surface ground were monitored during the model tests, and the changes in water content, particle-size and pore-size distributions in different positions after the model tests were measured and discussed. It is found that water content of the waste slurry without APAM flocculation changed from 204 to 195% by 24 hours standing and 15 hours vacuum preloading, while the water content of the waste slurry with APAM flocculation was declined from 163 to 96% by 24 hours standing, and was further reduced into 37% by 136 hours vacuum preloading, which shows that the combined method is feasible and effective.

• 한국미생물·생명공학회지
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• 제27권4호
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• pp.298-303
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• 1999

An $\alpha$-D-galactosidase ($\alpha$-D-galactoside galactohydrolase, EC 3. 2. 1. 22) from earthworm was purified by affinity chromatography using N-$\varepsilon$-aminocaproyl-$\alpha$-D-galactopyranosylamine coupled to sepharose and its properties were examined. The specific activity of the purified enzyme, tested with p-nitrophenyl-$\alpha$-D-galactopyranoside as substrate, was 314 units/mg protein, representing an 122-fold purification of the original crude extract. The final preparation obtained from by Sephadex G-25 chromatography showed a single band on SDS-polyacrylamide gel electrophoresis. The molecular weight was determined to be 48,000 by SDS-polyacrylamide gel electrophoresis. The purified galactosidase was showed maximum activity at pH 4.5 and 4$0^{\circ}C$, and was stable in the pH and temperature ranges from 4.0 to 5.5 and 30 to 5$0^{\circ}C$, respectively. The enzyme activity was inhibited by Zn2+, Hg2+ and Co2+. When the purified $\alpha$-galactosidase treated to guar gum for 6 hour, gel-promoting property was increased. It was clear that enzymatic elimination of galactose from guar gum by purified $\alpha$-galactosidase would lead to a significant increase in gelation ability.