• Proceedings of the PSK Conference
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• 2002.10a
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• pp.313.2-313.2
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• 2002

Environmentally benign protein staining method in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) using both an acidic dye, zincon (ZC) and a basic dye. ethyl violet (EV) is described. It is based on a counter ion-dye staining technique that employs oppositely charged two dyes to form an ion-pair complex. The selective binding of the free dye molecules to proteins in an acidic solution produces bluish violet colored bands. It is a rapid procedure, involving only fixin and staining steps that are completed in 45 min. (omitted)

• The Korean Journal of Food And Nutrition
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• v.37 no.1
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• pp.48-56
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• 2024

Effects of glutamic acid (Glu) and monosodium glutamate (MSG) on oxidative stability of oil-in-water (O/W) emulsions with different emulsifier charges during riboflavin (RF) photosensitization were evaluated by analyzing headspace oxygen content and conjugated dienes. Cetyltrimethylammonium bromide (CTAB), Tween 20, and sodium dodecyl sulfate (SDS) were used as cationic, neutral, and anionic emulsifiers, respectively. Glu acted as an antioxidant in CTAB- and Tween-20-stabilized O/W emulsions during RF sensitization, whereas Glu acted as prooxidants in SDS-stabilized O/W emulsions in the dark. However, adding MSG did not have a constant impact on the degree of oxidation in O/W emulsions irrespective of the emulsifier charge. In RF-photosensitized O/W emulsions, the emulsifier charge had a greater influence on antioxidant properties of Glu than on those of MSG.

• Journal of Microbiology
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• v.33 no.3
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• pp.244-251
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• 1995

An extracellular protease of Salmonella schottmulleri was purified from culture filtrate by using 0-75% ammonium sulfate precipitation, DEAE Sepharose Fast Flow ion exchange chromatography, Ultrogel HA chromatography and Sephacryl S-200 HR molecular sieve chromatography. To measure enzyme activity, synthetic dipeptide substrate (CBZ-arg-arg-AFC) with low molecular weight was employed as substrate. The molecular weight of the purified enzyme was approximately 80 kDa when determined by gel filtration on Sephacryl S-200 HR and 73 kDa when estimated by SDS-PAGE. The isoelectric point was 5.45. The activity of the purified enzyme was inhibited by metal chelating agesnts such as EDTA and 1.10-phenanthroline. The divalent cations, such as Ca$\^$2+/, Zn$\^$2+/, Fe$\^$2+/, Mg$\^$2+/ enhanced its activity. These results suggested that it was a metalloprotease. It had a narrow pH optimum of 6.5-7.5 with a maximum at pH 7.0 and a temperature optimum of 40.deg.C. It was stable at least for 1 week at 40.deg.C and maintained its activity for 24 hours at 50.deg.C, but it was rapidly inactivated at 65.deg.C. This protease was shown to be sensitive to sodium 50.deg.C, but it was rapidly inactivated at 65.deg.C. This protease was shown to be sensitive to sodium 50.deg.C, but it was rapidly inactivated at 65.deg.C. This protease was shown to be sensitive to sodium 50.deg.C, but it was rapidly inactivated at 65.deg.C. This protease was shown to be sensitive to sodium dodecyl sulfate (SDS) and was inactivated in a dose-dependent manner. However, it was resistant to Triton X-100 and the activity was enhanced to 32.3% with treatment of 0.025% Triton X-100.

• Food Science and Biotechnology
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• v.15 no.2
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• pp.324-327
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• 2006

The food-borne pathogen Listeria monocytogenes is commonly associated with meats and unpasteurized dairy products. To identify this pathogen in meats more efficiently than has been done in the past, we purchased meats from Korean markets and performed sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and serotyping analysis on Listeria organisms isolated from meat samples. Each Listeria species showed specific protein band patterns on SDS-PAGE. Whole-cell protein SDS-PAGE profiles indicated that the organisms isolated from meats sold in local Korean markets were L. monocytogenes with the serotypes 1/2a, 1/2b, 1/2c, and 4b. We suggest that it is possible to carry out molecular subtyping of L. monocytogenes using SDS-PAGE.

• Advances in environmental research
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• v.5 no.4
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• pp.213-224
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• 2016

This paper presents a numerical model based on a UTCHEM simulator to simulate surfactant flushing process to remediate diesel contaminated sand column. For this purpose, we modeled remediation process under 10000 and 20000 ppm initial concentrations of diesel. Various percent-mass sodium dodecyl sulfate (SDS) considered in our model. The model results indicated that 0.3 percent-mass of SDS at 10000 ppm and 0.1 percent-mass of SDS at 20000 ppm initial diesel concentration had maximum removal perdition which is in agreement with the experiment results. For 10000 ppm diesel concentrations, the coefficient of determination ($R^2$) and index of agreement (IA) between the model result and the experimental data were 0.9952 and 0.9695, respectively, and for 20000 ppm diesel concentrations, $R^2$ and IA were 0.9977 and 0.9935, respectively. The sensitivity analysis of permeability illustrated that in all diesel concentrations and SDS percent-mass with increasing permeability the model resulted in more removal efficiency.

• Bulletin of the Korean Chemical Society
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• v.25 no.9
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• pp.1321-1325
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• 2004

Sodium dodecyl sulfate (SDS), an anionic surfactant, can strongly adsorb at the surface of a carbon paste electrode (CPE) via the hydrophobic interaction. In pH 3.0 $Na_2HPO_4$-citric acid buffer (Mcllvaine buffer) and in the presence of SDS, the cationic indole-3-acetic acid (IAA, $pK_a$ = 4.75) was highly accumulated at the CPE surface through the electrostatic interaction between the negative-charged head group of SDS and cationic IAA, compared with that in the absence of SDS. Hence, the oxidation peak current of IAA increases greatly and the oxidation peak potential shifts towards more negative direction. The experimental parameters, such as pH, varieties of surfactants, concentration of SDS, and scan rate were optimized for IAA determination. The oxidation peak current is proportional to the concentration of IAA over the range from $5\;{\times}\;10^{-8}$ mol/L to $2\;{\times}\;10^{-6}$ mol/L. The detection limit is $2\;{\times}\;10^{-8}$ mol/L after 3 min of accumulation. This new voltammetric method was successfully used to detect IAA in some plant leaves.

• Journal of Soil and Groundwater Environment
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• v.16 no.5
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• pp.90-96
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• 2011

Simultaneous removal of heavy metals (Cd, Pb) and diesel-fuel from a soil column was evaluated by respectively flushing with sodium dodecyl sulfate (SDS) solution, mixture of SDS and sodium iodide (SDS + NaI), and surfactant foam (SDS + NaI foam). First, this study evaluated these flushing methods to the heavy metals only-contaminated soil for removal of heavy metals from the heavy-metal only contaminated soil column. After 7 pore volume flushing of the soil column, Cd removal efficiencies from the soil were 40% by SDS solution, 50% by SDS + NaI mixture, and 60% by surfactant foam. The flushing results implied that anionic surfactant and ligand can be efficiently applied to extraction of Cd from the heavy metal contaminated soil. Furthermore, surfactant foam flushing showed an increased flushing efficiency with enhancing the contact between surfactant solution and soil. However, Pb removal efficiency by these flushing methods did not show any difference unlike those of Cd. Second, this study eventually evaluated flushing methods for simultaneous removal of heavy metals and diesel-fuel from the soil column with 7 pore volume flushing. Diesel-fuel removal efficiencies were 50% by SDS + NaI flushing and 90% by SDS + NaI foam flushing. Cd removal efficiency by the foam flushing reached to 80% which was higher than the result of the previous heavy metals onlycontaminated soil experiment. This result implied that diesel-fuel could act as a metal-solvent while it contacted to heavy metals present in the soil. This study clearly showed that surfactant foam flushing simultaneously removed heavy metals and diesel fuel from the soil column.

• Journal of the Korean Society of Clothing and Textiles
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• v.11 no.2 s.24
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• pp.101-112
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• 1987

The purpose of this study is to investigate the influence of addition of sodium dodecyl sulfate(SDS) when wool is treated with sodium hydroxide(NaOH). Physical and chemical changes were examined on wool treated with various cone. of NaOH and SDS simultaneously. The result are as follows. 1. The higher the temperature and the longer the time of NaOH treatment are, the more alkali damage wool get : increase in weight loss and decrease in urea-bisalphite solubility and in tensile strength. But the treatment time reacts less effective than the temperature. 2. When wool is treated with NaOH, at NaOH cone. under $10^{-3}M$., the addition of SDS alleviates the alkali reaction on wool: increase in cystine contents and in urea-bisulpite solubility, and decrease in degree of swelling. On the other hand, at NaOH cone. over $10^{-2}M$., the addition of SDS promotes the alkali reaction on the wool. 3. When wool is treated with NaOH, the addition of SDS shows no changes on the tensile strength. On the other hand, at NaOH cone. under $10^{-2}M$., the addition of SDS shows no changes on the softness of wool, but at the $10^{-1}M$. NaOH cone. addition of SDS increases the soft-ness of wool. The area shrinkage of wool treated with NaOH and SDS shows less changes than with NaOH only.

• BMB Reports
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• v.37 no.4
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• pp.387-393
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• 2004

The L-asparaginase (E. C. 3. 5. 1. 1) enzyme was purified to homogeneity from Pseudomonas aeruginosa 50071 cells that were grown on solid-state fermentation. Different purification steps (including ammonium sulfate fractionation followed by separation on Sephadex G-100 gel filtration and CM-Sephadex C50) were applied to the crude culture filtrate to obtain a pure enzyme preparation. The enzyme was purified 106-fold and showed a final specific activity of 1900 IU/mg with a 43% yield. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of the purified enzyme revealed it was one peptide chain with $M_r$ of 160 kDa. A Lineweaver-Burk analysis showed a $K_m$ value of 0.147 mM and $V_{max}$ of 35.7 IU. The enzyme showed maximum activity at pH 9 when incubated at $37^{\circ}C$ for 30 min. The amino acid composition of the purified enzyme was also determined.

• Journal of the Korea Academia-Industrial cooperation Society
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• v.17 no.10
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• pp.199-203
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• 2016

Apolipophorin-III (apoLp-III) was isolated and purified from the last larval hemolymph of Galleria mellonella by KBr gradient ultracentrifugation and gel chromatography (Sephadex G-100). After KBr gradient ultracentrifugation, the lipophorin-free fractions were used as the samples for gel chromatography. The purity of the finally purified apoLp-III was confirmed by SDS-PAGE after gel chromatography. In this study, we found that apoLp-III is taken up into the adult testes in Galleria mellonella. The testes were dissected from day-1 or -2 adults in cold Ringer's solution and used for tissue culture. The protein moiety of apoLp-III was labeled with FITC dissolved in dimethyl sulfoxide (DMSO) at room temperature under conditions of continuous stirring for 1 h. The FITC-labeled apoLp-III was purified with a Sephadex G-25 PD-10 column. The tissues of the adult testes were incubated at room temperature for 30 min with fluorescein isothiocyanate (FITC)-labeled apoLp-III. Fluorescein microscopy and sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE) revealed that the adult testis tissues internalize the FITC-labeled apoLp-III. The results showed that apoLp-III is taken up by the adult testes.