• Applied Biological Chemistry
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• v.41 no.1
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• pp.23-30
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• 1998

The cryIB, truncated cryIB$[cryIB({\alpha})]$, cryIA(b), and cytA genes, encoding 135-, 89-, 131-, and 27-kDa proteins, respectively, from Bacillus thuringiensis were cloned into a shuttle vector pBES and expressed in E. coli and Bacillus species. The morphology and solubility in alkaline buffer of the insecticidal crystal proteins were investigated. Transformation of intact cells of E. coli and Bacillus species was achieved by electroporation. High field strength of 11.0 kV/cm and resistance of 129 ohms were required for efficient transformation of E. coli strains and 4.5 kV/cm and 48 ohms for Bacillus species. Strains of recombinant E. coli and Bacillus species produced the insecticidal crystal proteins and accumulated as the same bipyramidal and irregular structures as those of CryIB and IA(b) and CytA of B. thuringiensls, respectively. The insecticidal crystal proteins accumulated in recombinant E. coli wire smaller in size than those in recombinant Bacillus species. The solubility in alkaline buffer of the insecticidal crystal proteins of recombinant E. coli increased gradually as the pH increased, whereas in the case of Bacillus species the solubility increased gradually as the pH increased up to 9 and then the solubility increased greatly up to two times higher than that of E. coli proteins.

• Journal of Pharmaceutical Investigation
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• v.22 no.2
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• pp.105-113
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• 1992

To improve the solubility and dissolution rate of trimethoprim (TMP), which is slightly soluble drug, its inclusion complexes were prepared and studied in this experiment. Inclusion complexes of TMP with ${\beta}-cyclodextrin$ and ${\beta}-cyclodextrin$ polymer (CDPS) were prepared according to Fenyvesi method. These were compared with TMP and its physical mixture with CDPS. Water, diluted hydrochloric acid and phosphate buffer solution were used as dissolution media. And accelerated stability test was studied at $50,\;70\;and \;80^{\circ}C$. It was found that solubility and dissolution rate of inclusion complexes were increased in water. Especially, the solubility and dissolution rate of TMP was found to be markedly increased by inclusion complexation with CDPS. In stability test, ${\beta}-cyclodextrin$ inclusion complexes were more or less stable than TMP alone. This tendency was not led in CDPS. Consequently, CDPS was useful in increasing dissolution rate and stability of TMP.

• Journal of Pharmaceutical Investigation
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• v.29 no.3
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• pp.205-210
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• 1999

To formulate the parenteral delivery of a new cephalosporin derivative, 7-${\beta}$-[(2)-2-(2-arninothiazol-4-yl)-2methoxyiminoacetamido]- 3- [(2,3-cyclopenteno-4-carbamoyl-l-pyridinium)methyl]- 3-cephem-4-carboxylate sulfate( CKD604), the stability and solubility of CKD-604 in various aqueous media were investigated. The degradation kinetics of CKD-604 in aqueous solutions (ionic strength 0.1, pH 1-8) were studied at $37^{\circ}C$. The observed degradation rates followed pseudo first order kinetics. The pH-rate profile exhibited a minimum degradation rate at pH 5. The Arrhenius activation energy was 14.2 kcal/mol in pH 5 buffer solution. Excellent agreement between the cephalosporins' theoretical pH-rate profile and the experimental data indicated that the degradation pathway of CKD-604 could be predicted according to the general pathway of cephalosporins. The solubility of CKD-604 was 8.16 mg/ml at $25^{\circ}C$. To enhance the solubility and adjust the suitable pH, CKD-604 was solubilized by using sodium ascorbate, ascorbic acid and urea. The compositions were obtained to satisfy optimum pH and concentration, and the total amount of additives was several times of the active ingredient, CKD-604.

• Molecules and Cells
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• v.20 no.1
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• pp.119-126
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• 2005

${\alpha}$-Expansins are bound to the cell wall of plants and can be solubilized with an extraction buffer containing 1 M NaCl. Localization of ${\alpha}$-expansins in the cell wall was confirmed by immunogold labeling and electron microscopy. The subcellular localization of vegetative ${\beta}$-expansins has not yet been studied. Using antibodies specific for OsEXPB3, a vegetative ${\beta}$-expansin of rice (Oryza sativa L.), we found that OsEXPB3 is tightly bound to the cell wall and, unlike ${\alpha}$-expansins, cannot be solubilized with extraction buffer containing 1 M NaCl. OsEXPB3 protein could only be extracted with buffer containing SDS. The subcellular localization of the OsEXPB3 protein was confirmed by immunogold labeling and electron microscopy. Gold particles were mainly distributed over the primary cell walls. Immunohistochemistry showed that OsEXPB3 is present in all regions of the coleoptile and root tissues tested.

• Proceedings of the Korean Society of Soil and Groundwater Environment Conference
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• 2000.05a
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• pp.121-124
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• 2000

In-situ soil remediation using electrokinetics has been investigated and the attempts for the removal of hydrocarbons have been continued. In this study, the electrokinetic remediation using three different kinds of surfactnats was conducted for the removal of phenanthrene from clay The used surfactnats were APG, Brij30 and SDS. In the solubility test for phenanthrene, the experimental result was APG

• Korean Journal of Food Science and Technology
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• v.33 no.6
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• pp.769-773
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• 2001

Protein content of okara and soybean were found to be 37.3% and 42.5%, respectively by micro-Kjeldahl analysis. Solubility of okara protein in phosphate buffer (pH 8) was 10% versus soy protein of 68.4%. Insolubilization of okara protein was mostly due to disulfide bonding between cysteine residues caused by excessive heat treatment during soymilk processing: hydrophobic interactions and hydrogen bondings were involved to lesser extent. Optimum extraction temperature and time were $60^{\circ}C$ and 40 min. Typical solubility profile of soy protein disappeared for okara protein though minimum solubility of the protein was around pH 3.0. Treating okara with protease was effective in solubilizing okara protein and solubility increased to 19.2%. Optimum reaction temperature and time were $80^{\circ}C$ and 50 min, respectively. Cell wall degrading enzyme did not increase solubility of the protein, however. Through enzymatic reaction okara protein could be effectively solubilized for uses as food ingredient.

• Journal of Pharmaceutical Investigation
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• v.28 no.2
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• pp.121-126
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• 1998

The solubility and physicochemical stability of caroverine hydrochloride (CRV), an antispasmodic, in buffered aqueous solutions were studied using a reverse phase high performance liquid chromatography. The solubilty of the drug at pH 2.76-5.40 was similar at the range 31.9-36.2 mg/ml $(34^{circ}C)$, but, at the pH higher than 6.0, markedly decreased. The use of polyethylene glycol 400 as a cosolvent did not increase the solubility at any compositions examined. Moreover. increasing molar concentration of aqueous phosphate buffer from 0 to 0.5 M remarkably decreased the solubility. The degradation of CRY followed the apparent first-order kinetics. The degradation was accelerated with decreasing pH and increasing storage temperature. The half-lives for the degradation of CRY (1.0 mg/ml) at pH 1.28. 4.01 and 5.93 $(45^{\circ}C)$ were 2.8, 31.4 and 124 hr. respectively. The pHs of incubated solutions were to some extent lowered perhaps due to the formation of acidic degradation products. The addition of disodium edetate (0.01%) to the CRY solution (pH 4.95) retarded 2.5 times the degradation rate at $45^{\circ}C$, but the use of sodium bisulfite (0.1%) accelerated 2.9 times the rate. The activation energy for the CRY solution (20 mg/ml. pH 5.4) containing 0.01% EDTA was calculated to be 5.98 kcal/mole. When the solution was stored under nitrogen displacement in ampoule, there was no significant degradation even after 3 months at $40^{\circ}C$, indicating that protection from oxidation by air (oxygen) is essential for the complete stabilization of CRY solution.

• 한국정보디스플레이학회:학술대회논문집
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• 2009.10a
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• pp.791-793
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• 2009

We have developed novel small molecular materials for solution phosphorescent OLEDs having multilayered device structures. These novel materials are applied as an interlayer which is between a buffer layer (or hole injection layer) and an emitting layer to improve the luminance efficiency of solution green phosphorescent OLEDs. In order to form stable double layers by spincoating process, we take the advantage of solubility differences of interlayer materials and emitting materials. Using CIM3 as an interlayer, we have attained the best luminance efficiency, 36 cd/A at a given constant of 2000cd/$m^2$ in the structure of ITO/PEDOT:PSS/CIM3/CIM6:Ir(mppy)$_3$/BAlq/Alq$_3$/LiF/Al.

• Journal of Photoscience
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• v.7 no.2
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• pp.47-52
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• 2000

The copolymmers of N, N-dimethylaminoethyl methacrylate(DAEM) and N-arylmethacrylamide (AMA) were prepared, and their photochemical properties as a negative photoresist were studied by the measurements of insoluble fraction, and by UV and IR absorption spectral changes. These copolymers are soluble in DMF, actone, methanol, of acidic buffer solutions. Solubility of these copolymer films in the vuffer solutions increased with the amount of DAEM units in the copolymer and decreased with the pH value. The insoluble fraction of the copolymer films in the buffer solution of pH 4 of in methanol increased with irradiation time and the amount of AMA units in the copolymer. UV and IR spectral changes indicated that not only photo-crosslinking but also the photo-Fries rearrangement took place upon irradiation with a 254nm UV light.

• Journal of Pharmaceutical Investigation
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• v.17 no.3
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• pp.127-133
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• 1987

Dissolution characteristics and urinary excreted amount of commercially available three brands of sulfisoxazole tablets were investigated in order to elucidate the in vitro-in vivo correlations and relative bioavailability in humans. All the tablets tested met the K.P. IV and the USP XXI specifications for tablet weight variation, content uniformity, disintegration and dissolution. The disintegration and dissolution rate constants of sulfisoxazole tablets in pH 2.0 HCl-KCl buffer were reduced more significantly (p<0.05) than those in diluted HCl $(1{\rightarrow}12.5)$ and pH 6.5 phosphate buffer. It seemed to be attributed to the pH dependent solubility of sulfisoxazole. We could see that the relative bioavailability of brand B to sulfisoxazole powder was about 90% and that its value was higher than those of other two brands from the urinary excretion data obtained from eight healthy male volunteers by means of Latin square cross over design. No useful correlation was observed between the in vitro and in vivo studies in this experiment.