• Title, Summary, Keyword: Purification

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Investigation of the Hydraulic Stability of Agricultural Drainage Channels Installed Water Purification Materials by using Flow-3D (Flow-3D를 활용한 수질정화체가 설치된 농업용 배수로의 안정성 조사)

  • Kim, Sun-Joo;Park, Ki-Chun
    • Journal of The Korean Society of Agricultural Engineers
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    • v.49 no.5
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    • pp.3-9
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    • 2007
  • In this study, the effect of the purification materials is analyzed and tested by Flow 3D and Hydraulic model test. Three dimension numerical analysis led from the research that sees abnormal form and the size back of the water purification material conferred the flowing water conduct inside the test channel against the test condition. Comparison it analyzed the flux distribution, a water depth of the channel which establishes the water purification materials the cross section, an interval of the water purification material, a conference with general channel, it change executed. As a result, the cross section ratio of the purification materials against and a flux change from the test which it sees. The interval of the purification materials in order to prevent three dimension that follows in decrease of increase and flux must decide an interval.

A Novel Purification Process for Homoharringtonine from Celphalotaxus koreana

  • Sung, Ju-Li;Kim, Jin-Hyun
    • 한국생물공학회:학술대회논문집
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    • pp.521-524
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    • 2003
  • An effective purification method was developed for producing Homoharringtonine (HHT), to guarantee high purity and yield from Cephalotaxus koreana. This process was a simple and efficient procedure, for the isolation and purification of HHT form the biomass of Cephalotaxus koreana, consisting of extract, adsorbent treatment, precipitation and followed by a chromatography. The extraction, adsorbent treatment and precipitation in pre-purification process allows for rapid and efficient separation of HHT from many compound and dramatically increases the yield and purity of crude HHT for HPLC purification steps compared to alternative processes. This purification processes serves to minimize solvent usage, size, and complexity of the operations for HHT purification.

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Determination of self-purification constants and regulation of pollutants loaded in the ecosystems (生態系에 있어서 自淨係數의 測定과 汚染負荷量의 調節 原理)

  • Chang, Nam-Kee;Kim, Jae-Young
    • The Korean Journal of Ecology
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    • v.15 no.3
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    • pp.287-296
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    • 1992
  • To determinate self-purification constants of pollutants loaded in the ecosystems, the self- purification process was formulated, and a measurement method of the self-purification constants was derived. $C=C_0e^{-st}$ When $C_0$ is the initial pollutant amounts loaded in a ecosystem, and C is the rest pollutant amounts after the time, t, the equation of the self-purification, s, is $s=\frac{P}{C}$ When in aquatic ecosystem, $C_0$ is the initial polluant amounts loaded in water body, and Cis the rest pollutation amounts after the time, t, the self-purification constant, s, is $s=(\frac{\ln C_0-\ln C}{t}$ Self-purification constants of pine and oak forests at kwangneung in kyonggido were 0.07 and 10 respectively, of BOD in gokneung stream in kyonggido was 0.51, and of glucose and phosphate in pools on the stone in mt.jiri were 0.49 and 15.19 respectively.

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Paclitaxel : Recovery and Purification in Commercialization Step (Paclitaxel : 산업화 단계에서의 회수 및 정제)

  • Kim Jin-Hyun
    • KSBB Journal
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    • v.21 no.1
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    • pp.1-10
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    • 2006
  • The recovery and purification of a paclitaxel from plant cell cultures is essential to commercial process. This review describes a large-scale recovery and purification method for producing paclitaxel, to guarantee high purity and yield from plant cell cultures. Also, the process of separation and purification is optimized in conjunction with a extraction step, pre-purification, purification, and polishing (drying) as an integrated process to meet final product quality requirements such as purity, residual solvents, product morphologies, impurities, bacterial endotoxin, etc. This information is very useful for production and quality control of pharmaceuticals in commercialization step.

Retrospective analyses of the bottleneck in purification of eukaryotic proteins from Escherichia coli as affected by molecular weight, cysteine content and isoelectric point

  • Jeon, Won-Bae
    • BMB Reports
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    • v.43 no.5
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    • pp.319-324
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    • 2010
  • Experimental bioinformatics data obtained from an E. coli cell-based eukaryotic protein purification experiment were analyzed in order to identify any bottleneck as well as the factors affecting the target purification. All targets were expressed as His-tagged maltose-binding protein (MBP) fusion constructs and were initially purified by immobilized metal affinity chromatography (IMAC). The targets were subsequently separated from the His-tagged MBP through TEV protease cleavage followed by a second IMAC isolation. Of the 743 total purification trials, 342 yielded more than 3 mg of target proteins for structural studies. The major reason for failure of target purification was poor TEV proteolysis. The overall success rate for target purification decreased linearly as cysteine content or isoelectric point (pI) of the target increased. This pattern of pI versus overall success rate strongly suggests that pI should be incorporated into target scoring criteria with a threshold value.

A New large-scale Pre-purification for Peroxidase from Plant Cell Cultures (식물세포 배양으로부터 Peroxidase 대량 정제를 위한 전처리 공정 개발)

  • 표상현
    • KSBB Journal
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    • v.15 no.4
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    • pp.342-345
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    • 2000
  • A novel pre-purification method was developed for producing peroxidase to guarantee high purity and yield from plant cell cultures in large-scale process. This method was a simple and efficient procedure for the isolation and pre-purification of peroxidase from the biomass consisting of active clay treatment followed by cationic exchange chromatography. The use of active clay in the pre-purification process allows for rapid and efficient separation of peroxidase from interfering compounds and dramatically increases yield and purity of crude peroxidase for purification steps compared to alternative processes. This pre-purification process serves to minimize the buffer usage size and complexity of the HPLC operations for peroxidase purification. This process is readily scalable to a pilot plant and eventually to a production environment where mass production of material are expected to be produced.

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A Photosensitive Glass Chip for DNA Purification of Nucleic Acid Probe Assay

  • Kim, Joon-Ho;Kim, Byung-Gyun;Yoon, Jun-Bo;Euisik Yoon
    • JSTS:Journal of Semiconductor Technology and Science
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    • v.1 no.4
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    • pp.232-238
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    • 2001
  • A new DNA purification chip is proposed and fabricated for the sample preparation of Nucleic Acid (NA) probe assay. The proposed DNA purification chip is fabricated using photosensitive glass substrate and polydimethylsiloxane (PDMS) cover fixture. We have successfully captured and eluted the DNA using the fabricated photosensitive glass chip. The fabricated DNA purification chip showed a binding capacity of $15ng/\textrm{cm}^2$and a minimum extractable input concentration of $100copies/200\muL$. The proposed DNA purification chip can be applied for low-cost, disposable sample preparation of NA probe assays.

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Purification of Radiolabeled RNA Using Sephadex G-15 or G-50 Chromatography (Sephadex G-15 또는 G-50 chromatography를 이용한 방사성 동위원소로 표지된 RNA의 정제)

  • Yoo, Beong-Gyu;Lee, Jong-Seok
    • Journal of radiological science and technology
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    • v.21 no.1
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    • pp.65-68
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    • 1998
  • We attempted to purify radiolabeled RNA using Sephadex G-15 and G-50 chromatography instead of commercial RNA purification kit. In the Sephadex G-15 chromatography the major portion of RNA was eluted in the fractions ranging from 3rd to 5th whereas broad elution profile of RNA was obtained from the Sephadex G-50 chromatography. The elution profile and purity of RNA obtained from Sephadex G-15 chromatography was very similar to that by commercial RNA purification kit. Furthermore, operating time required for purification of RNA by Sephadex G-15 was rather smaller than that by commercial kit. Overall results suggest that the purification of radiolabeled RNA using Sephadex G-15 is more money and time saying than using commercial RNA purification kit.

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Novel Purification Method of Kv 4.2 Potassium Channel from Rat Brain Membrane

  • Park, Sung-Soo
    • Biomedical Science Letters
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    • v.18 no.2
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    • pp.96-103
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    • 2012
  • Kv 4.2 ion channel protein has an ability to open at subthreshold membrane potentials and to recover quickly from inactivation. That is very important for neuronal signal transmission in vertebrate brain. In order to purify Kv 4.2 protein, the novel purification methods were experimented. The purification procedure utilized chromatography on DE-52 ion exchange column and affinity chromatography on a WGA-Sepharose 4B, and Kv 4.2 affinity column chromatography. It was found that 0.5% (wt./vol.) Triton X-100 detergent in lysis buffer worked well for Kv 4.2 protein solubilization from rat brain membrane. Protein quantitative determination was conducted by BCA method at 562 nm for each purification step to avoid determination interference of protein at 280 nm by detergent. The confirmation of Kv 4.2 existence and amount is performed using by SDS-PAGE/immunoblotting or 96-well dot blotting. The Kv 4.2 without interacting protein that contains carbohydrate, was purified from novel biochemical 3-steps purification method for further research.

Isolation and purification of chicken egg yolk immunoglobulin against Edwardsiella tarda (Edwardsiella tarda에 대한 계란난황항체의 분리와 정제)

  • Kim, Yeong-Dae;O, Myeong-Ju;Jeong, Tae-Seong;Jeong, Seong-Ju
    • Journal of fish pathology
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    • v.17 no.1
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    • pp.11-20
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    • 2004
  • The present study compared purification methods of hen egg yolk immunoglobulin (IgY) from the hen immunized with Edwardsiella tarda. The purification of anti-E. tarda IgY was performed by four different methods, polyethylene glycol (PEG), chloroform polyethylene glycol (Chloroform-PEG), ammonium sulfate and purification kit. Purified IgY had heavy chain of 64 kDa and light chain of 27 kDa size. IgY purified from the hen immunized with E. tarda showed higher ELISA values and agglutination titers than those with IgY purified from the non-immunized hen as a negative control. In addition, purified IgY recognized similar E. tarda proteins to those with anti-E. tarda rabbit serum by western blotting. Purified IgY had an agglutination titer of 1:512 by PEG method and ammonium sulfate method, and 1:128 by chloroform-PEG method and purification kit. Moreover, PEG method was the most rapid method among the four different IgY purification methods. These results indicate that PEG method is effective purification method maintaining biological activity of the IgY.