• Journal of the Korean Chemical Society
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• v.55 no.2
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• pp.163-168
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• 2011

The variations of molar conductivity of various surfactants such as sodium caprylate, sodium laurate, sodium palmitate, sodium stearate, sodium oleate, sodium dodecyl sulphate, and lithium dodecyl sulphate with concentrations of the surfactants for each of the solutions consisting of mixtures of varying concentrations of N-methyl acetamide in water at constant temperature of $30{\pm}0.2^{\circ}C$ were studied. The critical micelle concentration (CMC) for each surfactant is measured. It is found that the CMC values in mixtures of N-methyl acetamide and water solutions of various surfactants are lower than the CMC values in water, and the driving force for micelle formation correlates with solvophobicity. The surfactant-solvent interactions that drive amphiphilic self-organization in N-methyl acetamide in water are discussed. Thermodynamic parameters were evaluated for micellar system to explain the results.

• BMB Reports
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• v.35 no.4
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• pp.364-370
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• 2002

The effect of sodium n-dodecyl sulphate (SDS) on hemoglobin autoxidation was studied in the presence of a 100mM phosphate buffer (pH 7.0) by different methods. These included spectorphotometry, fluorescence technique, cyclic voltametry, differential scanning calorimetry, and densitometry. Spectroscopic studies showed that SDS concentrations up to 1 mM increased deoxy-, decreases oxy-, and had no significant effect on the met- conformation of hemoglobin. Therefore, a SDS concentration up to 1 mM increased the deoxy form of hemoglobin as the folded, compact state and decreases the oxy conformation. The turbidity measurements and differential scanning calorimetry techniques indicated a more stable conformation for hemoglobin in the presence of SDS up to 1mM. Electrochemical studies also confirmed a more difficult oxidation under these conditions. The induction of the deoxy form in the presence of SDS was confirmed by densitometry techniques. The compact structure of deoxyhemoglobin blocks the formation of met-conformation in low SDS concentrations.

• BMB Reports
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• v.39 no.5
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• pp.530-536
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• 2006

Thermal conformational changes of human serum albumin (HSA) in phosphate buffer, 10 mM at pH = 7 are investigated using differential scanning calorimetric (DSC), circular dichroism (CD) and UV spectroscopic methods. The results indicate that temperature increment from $25^{\circ}C$ to $55^{\circ}C$ induces reversible conformational changes in the structure of HSA. Conformational change of HSA are shown to be a three-step process. Interestingly, melting temperature of the last domain is equal to the maximum value of fever in pathological conditions, i.e. $42^{\circ}C$. These conformational alterations are accompanied by a mild alteration of secondary structures. Study of HSA-SDS (sodium dodecyl sulphate) interaction at $45^{\circ}C$ and $35^{\circ}C$ reveals that SDS affects the HSA structure at least in three steps: the first two steps result in more stabilization and compactness of HSA structure, while the last one induces the unfolding of HSA. Since HSA has a more affinity for SDS at $45^{\circ}C$ compared to $35^{\circ}C$, It is suggested that the net negative charge of HSA is decreased in fever, which results in the decrease of HSA-associated cations and plasma osmolarity, and consequently, heat removal via the increase in urine volume.

• BMB Reports
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• v.34 no.5
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• pp.415-420
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• 2001

Chloramphenicol acetyltransferase (CAT) was purified to homogeneity from Morganella morganii starting with ammonium sulphate fractionation, followed by separation on DEAE-Sephadex A50, and G-100 Sephadex gel filtration. The enzyme was purified 133.3 fold and showed a final specific activity of 60 units/mg protein with a yield of 37%. Sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) of the purified enzyme revealed it as a heterotetramer that consists of four subunits with close molecular weights (19.5, 19, 18, and 17.5 kDa). The molecular weight of the native enzyme was calculated to be 78 kDa, as determined by gel filtration, which approximated to that of the four subunits (74 kDa). The enzyme showed a maximum activity at pH 7.8 when incubated at $35^{\circ}C$. A Lineweaver-Burk analysis gave a Km of 5.0 uM and Vmax of 153.8 U/ml. The amino acid composition of the purified enzyme was also determined.

• YAKHAK HOEJI
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• v.38 no.1
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• pp.38-45
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• 1994

An analytical method using capillary electrophoresis (CE) was developed for quantitation of water soluble vitamin contents in various vitamin products. The method includes the optimization of separation of 11 water soluble vitamins changing the micellar concentration and pH of running buffer, applied voltage and sample preparation. Best resolution was obtained with 25 mM phosphate buffer (pH=8.0) containing 50 mM sodium dodecyl sulphate (SDS) as micellar phase. At optimum condition, water soluble vitamins were determined in orange juice and vitamin products such as vitamin C pulvis, vitamin injection, coated multivitamin tablet. The quantitative analysis of water soluble vitamins with CE was suitable for quality control of pharmaceutical products with sound reproducibility.

• 한국정보디스플레이학회:학술대회논문집
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• 2009.10a
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• pp.914-916
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• 2009

Using gelatin and acacia as wall and electronic ink as core substance, microcapsules were prepared by complex coacervation to fabricate a flexible electronic paper display. In order to obtain the microcapsules in a narrow dispersed distribution, we focus on the interfacial tension between the hydrophobic electrophoretic ink and an aqueous polyelectrolyte solution, through controlling sodium dodecyl sulphate (SDS) concentration and stirring rate. The existence of anionic surfactant of SDS not only decreases the droplet diameters, but also reduces the diameter size distribution. And, as the stirring rate is increased, the average size of microcapsule is also decreased.

• Polymer(Korea)
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• v.34 no.4
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• pp.306-312
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• 2010

Triphenylvinylsilane (TPVS) containing vinyl acetate (VAc), butyl acrylate (BA), and Nmethylolacrylamide (NMA) copolymers were prepared by emulsion polymerization. The polymerization was performed at $80^{\circ}C$ in the presence of auxiliary agents and ammonium peroxodisulfate (APS) as the initiator. Sodium dodecyl sulphate (SDS) and Arkupal N-300 were used as anionic and nonionic emulsifiers, respectively. The resulting copolymers were characterized by using Fourier transform infrared spectroscopy (FTIR), gel permeation chromatography (GPC), and dynamic light scattering (DLS). Thermal properties of the copolymers were studied by using thermogravimetric analysis (TGA) and differential scanning calorimetry (DSC). The morphology of copolymers was also investigated by scanning electron microscopy (SEM) and then the effects of silicone concentrations on the properties of the TPVS-containing VAc-acrylic emulsion copolymers were discussed. The obtained copolymers have high solid content (50%) and can be used in weather resistant emulsion paints as a binder.

• Preventive Nutrition and Food Science
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• v.9 no.3
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• pp.283-288
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• 2004

Superoxide dismutase (SOD) from tomato (Lycopersicon esculentum Mill.) fruit was purified by ammonium sulphate precipitation, Sephadex G-100 and DEAE-cellulose column chromatographies. A 22 fold purification and an overall yield of 44% were achieved. The purified enzyme was a homodimer with Mr 37.1 kDa and subunit Mr 18.2 kDa as judged by SDS-PAGE. SOD showed $K_{m}$ values of 25 ${\times}$ 10$^{-6}$ M and 1.7 ${\times}$ 10$^{-6}$ M for nitroblue tetrazolium (NBT) and riboflavin as substrates, respectively. The enzyme was thermostable upto 5$0^{\circ}C$ and exhibited pH optima of 7.8. The effect of metal ions and some other compounds on enzyme activity was studied. $Co^{2+}$ and $Mg^{2+}$ were found to enhance relative enzyme activities by 27 % and 73 %, respectively, while M $n^{2+}$ inhibited the SOD activity by 64%. However, $Ca^{2+}$ and C $u^{2+}$ had no effect on enzyme activity. Other compounds like $H_2O$$_2$ and Na $N_3$ inhibited enzymatic activities by 60% and 32%, respectively, while sodium dodecyl sulphate (SDS), chloroform plus ethanol and $\beta$-mercaptoethanol had no effect on the activity of SOD. of SOD.

• Asian-Australasian Journal of Animal Sciences
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• v.18 no.12
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• pp.1780-1785
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• 2005

Very low density lipoprotein (VLDL) of commercial broiler (CB) and crossbred village chicken (AK) was purified using Fast Protein Liquid Chromatography (FPLC). The fraction collected was then confirmed as VLDL using 4% polyacrylamide gel electrophoresis and transmission electron microscopy (TEM). The particle size of VLDL is 46.8${\pm}$8.6 nm. The VLDL fraction was then subfractionated and the apolipoprotein (apo) profile was studied by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDSPAGE). The CB and AK have almost similar types of apo in both subfractions 1 and 2. The AK showed the presence of apoAI, AIV, D and E whereas the CB had apo AIV, D, E and H. The apo AIV and apo E were present in both subfractions of AK and CB.

• Asian-Australasian Journal of Animal Sciences
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• v.24 no.12
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• pp.1666-1673
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• 2011

The presence of sialoglycoproteins (SGPs) in the membranes from goat (Capra aegagrus hircus), buffalo (Bubalus bubalis bubalis) and pig (Sus scrofa domestica) erythrocytes was investigated by partial purification with a chloroform-methanol extraction method followed by Sodium dodecyl sulphate - Polyacrylamide gel electrophoresis in comparison to human (Homo sapiens) erythrocytes. The results show that mammalian erythrocytes possess clear differences in the SGPs numbers and molecular weights although all animals studied in this experiment are from the same class i.e. mammalia. The SGPs number in human, goat, buffalo and pig are four (PAS-1 to PAS-4), ten (PAS-GI to PAS-GX), seven (PAS-BI to PAS-BVII) and four (PAS-PI to PAS-IV) respectively as indicated by staining the polyacrylamide gel with sialoglycoprotein-specific Periodic acid-Schiff's (PAS) stain. The new SGPs could be observed only after the partial purification of membrane fractions named as PAS-HI with molecular weight (Mr) 190 kDa and PAS-HII 150 kDa in human, PAS-BIA in buffalo and PAS-PIA and PAS-PIVA in pig. The gels were also stained with Coomassie brilliant blue (CBB) and Silver stain to check the contamination of other membrane proteins in the purified fractions. The quantitative distribution of SGPs was also determined by densitometry. Present study indicates that there are some basic differences in mammalian erythrocyte membrane SGPs, especially with respect to their number and molecular weights indicating major structural variations.