• Applied Chemistry for Engineering
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• v.10 no.1
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• pp.160-165
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• 1999

Agarose gels can be used as reference standards for the measurement of fluid properties in porous media because the relaxation properties of the gel reference standard and those of the fluid in porous media can be closely matched. The use of reference standard to determine porosity and saturation is discussed and the requirements for gel NMR properties given. The relaxtion times of agarose gels measured at 2.0 Tesla are illustrated as a function of agarose and paramagnetic impurity ($CuSO_4$) concentrations. This work shows an empirical result between agarose gel composition and gel relaxtion times. The average value for the porosity distribution is 17.7%, which compares well with the value calculated with the gravimetric analysis. Finally, two phase immiscible displacement using agarose gels as a reference standard was performed. The saturation profiles appear to be consistent with what one might calculate for a one-dimensional displacement in a uniform porous media.

• Korean Journal of Food Science and Technology
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• v.31 no.1
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• pp.110-114
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• 1999

The present study was conducted to investigate the preparative methods of agarose for gel electrophoresis from agar. Naturally occuring agar consists of two main polysaccharides, the neutral polysaccharide agarose and the acid sulphated polysaccharide agaropectin. The sulphate and carboxyl functions of the agar are accumulated in the agaropectin. The hydrophilic, non-ionogenic, rigid and transparent gel matrix of the agarose was found to be suitable for gel electrophoresis gel filtration and affinity chromatography. Agar was purified by chitosan treatment, cetylpyridinium chloride (CPC) treatment, and polyethylene glycol (PEG) treatment. Yields of agarose purified from agar with chitosan, CPC and PEG were 56.7%, 55.6% and 62.3%. It was proper to treat with chitosan in preparative methods of agarose for gel electrophoresis from agar.

• Korean Journal of Microbiology
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• v.21 no.4
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• pp.221-228
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• 1983

An improved procedure for the rapid purification of glucose-6-phosphate dehydrogenase from extracts of Saccharomyces cerevisiae was developed by using affinity chromatography. Among six affinty media tested, $NADP^+ -agarose$ and Affi-gel Blue were more effective than others (i.e., Affi-gel Red, AMP-agarose, ATP-agarose, and $NAD^+ -agarose$). Conditions to desorb the enzyme bound to the affinity media were examined to increase the purity as well as yield. The best result was obtained when the column was developed with a linear gradient of KCl (0-1.0M). In case of Affi-gel Blue, introduction of $NAD^+$ (15mM) washing step prior to the salt gradient was most effective to remove $NAD^+ -binding$ proteins. For a large scale preparation of G-6-P dehydrogenase higher recovery was obtained by Affi-gel Blue than $NADP^+ -agarose$, however, the purity of the enzyme was decreased by 10 times if the former was used as the affinity medium. The capacity of Affi-gel Blue for G-6-P dehydrogenase was found to be 5 times higher than that of $NADP^+ -agarose$. Furthermore Affi-gel Blue could be reused repeatedly and its preparation is relatively easier and less expensive than $NADP^+ -agarose$.

• Journal of the Korean Society of Visualization
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• v.11 no.1
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• pp.16-21
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• 2013

In this study, diffusion coefficients of 20 kDa FITC-dextran in 2% agarose gel with different cell concentrations were measured using fiberoptic-based fluorescence recovery after photobleaching technique. As increasing cell concentration suspended in agarose gel, the diffusion coefficients were decreased. The diffusion coefficient of agarose gel which contains $10{\times}10^6$ cells/ml was decreased to 11% that of in agarose gel without cells. The distribution of fluorescence dye in 3D scaffold was also simulated. The simulation result shows that the diffusion coefficient is more significant factor than the scaffold structure.

• Korean Journal of Microbiology
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• v.14 no.4
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• pp.176-185
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• 1976

An improved procedure for the rapid purification of glucose-6-phosphate dehydrogenase from extracts of Saccharomyces cerevisiae was developed by using affinity chromatography. Among six affinty media tested, NADP$^{+}$-agarose and Affi-gel Blue were more effective than others (i.e., Affi-gel Red, AMP-agarose, ATP-agarose, and NAD$^{+}$-agarose). Conditions to desorb the enzyme bound to the affinity media were examined to increase the purity as well as yield. The best result was obtained when the column was developed with a linear gradient of KCl (0-1.0M). In case of Affi-gel Blue, introduction of NAD$^{+}$ (15mM) washing step prior to the salt gradient was most effective to remove NAD$^{+}$-binding proteins. For a large scale preparation of G-6-P dehydrogenase higher recovery was obtained by Affi-gel Blue than NADP$^{+}$-agarose, however, the purity of the enzyme was decreased by 10 times if the former was used as the affinity medium. The capacity of Affi-gel Blue for G-6-P dehydrogenase was found to be 5 times higher than that of NADP$^{+}$-agarose. Furthermore Affi-gel Blue could be reused repeatedly and its preparation is relatively easier and less expensive than NADP$^{+}$-agarose.X> +/-agarose.

• Korean Journal of Microbiology
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• v.29 no.4
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• pp.221-225
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• 1991

The RNA transcripts produced from in vitro transcription reaction of BTV core were analyzed on agarose-urea gel. Fast migrating abortive RNAs, in addition to full length species of RNA, were observed. Fast migrating RNAs extracted from agarose-urea gel were hybridized to all 10 segments of genomic ds RNA, while solw migrating RNAs extracted from agarose-urea gel were hybridized only to the large and medium size genomic ds RNA. These results indicate that fast migrating RNA transcripts are most likely the products of abortive transcription.

• Microbiology and Biotechnology Letters
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• v.38 no.4
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• pp.428-433
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• 2010

Enzymatic hydrolysis of sulfate groups in agaropectin or agar simplifies the production process of high-quality or low sulfate-content agarose. This study was investigated that cell surface displayed arylsulfatase can be applied to desulfatation of agar for production of agarose. Sulfate content of agarose prepared by treatment of yeast surface-displayed arylsulfatase was decreased in a enzyme dosedependent manner. Especially, 35 unit/mL of yeast surface arylsulfatase attenuated sulfate content of agarose up to 0.2%. In the 0.6% agar(Junsei), 35 unit/mL enzyme treated at $40^{\circ}C$ for 3 h showed the lowest content of sulfate. Therefore, this result was determined to be the optimal condition to desulfatation of agar for production of agarose. In addition, the gel strength of yeast surface arylsulfatase treated agar and commercial agarose were compared. Agarose prepared by treatment of yeast surface arylsulfatase showed $559.8{\pm}0.12$ of gel strength, and it is a similar compared to the commercial agarose.

• Journal of Microbiology and Biotechnology
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• v.4 no.3
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• pp.235-236
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• 1994

Direct colony hybridization on agarose gel plate was established for the identification of recombinant plasmids. The hybridization of the probe to nucleic acids on dried gel without transferring to solid supports was more effective and simpler than hybridization of such probes to materials immobilized on filters such as nitrocellulose or nylon. D-cycloserine in overlaying agamse was essential for releasing the nucleic acids from colony.

• Journal of Electrochemical Science and Technology
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• v.13 no.3
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• pp.347-353
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• 2022

Agarose hydrogel, a solid electrolyte, was investigated voltammetrically in terms of transport properties and natural convection effects using a ferrocenyl compound as a redox probe. To confirm the diffusion properties of solute on the agarose interface, the diffusion coefficients (D) of ferrocenemethanol in agarose hydrogel were determined by cyclic voltammetry (CV) according to the concentration of agarose hydrogel. While the value of D on the agarose interface is smaller than that in the bulk solution, the square root of the scan rate-dependent peak current reveals that the mass transport behavior of the solute on the agarose surface shows negligible convection or migration effects. In order to confirm the reduced natural convection on the gel interface, scan rate-dependent CV was performed in the solution phase and on the agarose surface, respectively. Slow scan voltammetry at the gel interface can determine a conventional and reproducible diffusion-controlled current down to a scan rate of 0.3 mV/s without any complicated equipment.

• ALGAE
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• v.20 no.1
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• pp.61-67
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• 2005

Agar was extracted from Gelidium amansii, which was harvested at the shores of Jeju Island in South Korea. As a unique solvent, the ability of dimethyl sulfoxide (DMSO) was used to separate agarose from agar by removing agaropectine and quality of the resultant agarose was characterized for chromatography purposes. Agar sample was agitated by motor-driven stirrer with DMSO in a water bath (at 70$^{\circ}C$ for 2 h) and centrifuged (3,000 rpm for 20 min). Resultant upper agarose layer was gelled, washed, dried and milled. The quality of agarose was evaluated by the analysis of proximate chemical composition, sulfate content, gelling strength and DNA migration. In this study, the separated agarose showed low sulfate amount (0.28%) and showed high gel strength (1190 g ${\cdot}\;cm^{-2}$). The resolution power and the ligase activities gave clear picture about the suitability of the present agarose for practical purposes.