• Proceedings of the Korean Institute of Electrical and Electronic Material Engineers Conference
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• 2007.06a
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• pp.240-241
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• 2007

In general, high temperature superconducting coated conductors have intermediary buffers layer consisting of seed, diffusion barrier and cap layers. Simplification of the oxide materials buffer architecture in the fabrication of high temperature superconducting coated conductors is required because the deposition of multi-layers buffer architecture leads to a longer manufacturing time and a higher cost process of coated conductors. Thus, single buffer layer deposition seems to be important for practical coated conductor manufacturing process. In this study, a single gradient layered buffer deposition process of YZO for low cost coated conductors has been tried using DC reactive sputtering technique. About several thick YZO gradient single buffer layers deposited by DC co-sputtering process were found to act as a diffusion layer.

• Journal of Korean Institute of Industrial Engineers
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• v.21 no.4
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• pp.541-553
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• 1995

An efficient algorithm is proposed for a buffer allocation in a continuous flow line. The problem is formulated as a non-linear programming with linear constraints. The concept of pseudo gradient and gradient projection is employed in developing the algorithm. Numerical experiments show that the algorithm gives the actual optimal solutions to the problems with single linear constraint limiting the total buffer capacity. Also, even in longer production lines, it gives quite good solutions to the problems with the general linear resource constraints within a few seconds.

• Biotechnology and Bioprocess Engineering:BBE
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• v.8 no.1
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• pp.47-53
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• 2003

An experimental study on the chromatographic separation of maltopentaose from a mixture, including glucose, maltose, maltotriose, and maltopentaose, was carried out in a nonionic polymeric sorbent column while varying the operating conditions, such as the solution pH, buffer contents, and isopropyl alcohol (1PA) concentration. Unlike the pH and buffer contents, the IPA concentration had a Significant impact on the single component chromatograms for maltopentaose. The retention times of the maltooligosaccharides with the nonionic polymeric sorbent Sp207 were in the following order: glucose < maltose < maltotriose < maltopentaose. From the experimental binary, ternary, and quaternary chromatograms, gradient chromatographic separation with a changing IPA concentration as a function of time was required to obtain high-purity maltopentaose and reduce the elution time.

• Korean Journal of Food Science and Technology
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• v.20 no.6
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• pp.856-861
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• 1988

A new method developed for simultaneous purification of enterotoxin A and C from Staphylococcus aureus strain L 350/1 consisted of chromatography on carboxymethyl (CM)-cellulose using a buffer of variable pH, gel filtration on Ultro gel, and fast protein liquid chromatography(FPLC) using a buffer of variable pH. The enterotoxin A and C were purified by three steps: batchwise adsorption from culture supernatant on Amberlite CG-50; chromatography on CM-cellulose using a buffer of constant pH and molarity; and gel filtration on Sephadex G-75. The purified enterotoxin appeared homogeneous by gel diffusion and polyacrylamide gel electrophoresis. Upon treatment with CM-cellulose using a elution of variable pH, enterotoxin A and C were so close that they were not separated completely. After elution from gels, the enterotoxins appeared as a single peak at the same position. Gel filtration gave a reaction of complete identity to enterotoxin A and C in Ouchterlony immunodiffusion. In FPLC using a CM-cellulose, enterotoxin A and C were simultaneously separated at pH 8.6 and 6.8. When each fraction was performed to gel immunodiffusion, at peak of enterotoxin A and C were not detected each other. In a method of elution by pH-gradient was to be more efficient as a simultaneous separation method in terms of speed, yields and simplicity. The purified toxin A and C were identical to type A and C reference enterotoxin on both disc electrophoresis and Ouchterlony gel diffusion.

• Applied Biological Chemistry
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• v.2
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• pp.36-39
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• 1961

It has been ascertained that S-(1, 2-dichlorovinyl) L-cysteine (DCVC) is probably the toxic component in the trichloro-ethylene extracted soybean oil meal on the bovine. For the study of the metabolites of DCVC, the components with radioactive $S^{35}$-in the urine of the calf, to which $S^{35}$-DCVC was administrated, were separated using of cellulose powder with propanol-water (70:30 V/V) which is easily removable by evaporation. As the results followings were obtained: Peak 1, which shows fractions containing single $S^{35}$-radioactive components, whose Rf is 0.815 Peak 2, which shows fractions containing jingle $S^{35}$-radioactive component, whose Rf is 0.447 Peak 3, which shows fractions containing both $S^{35}$-radioactive components whose Rfs are 0.090 and 0.171 Peak 4, which shows fractions containing single $S^{35}$-radioactive component, whose Rf is 0.142. Peak 5, which shows fractions containing single $S^{35}$-radioactive component, whose Rf is 0.084. Besides these, two of small peak were obtained. Although, the resolving power of the cellulose powder column is not sufficient, it is applicable for the study of the components of metabolytes of DCVC conveniently with the rest of removable solvent easily. Also the components with radioactive $S^{35}$ in the feces of the calf were separated using citrate buffer gradient system of Moore and stein. As the results; three $S^{35}$-radioactive components were separated.

• Parasites, Hosts and Diseases
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• v.37 no.1
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• pp.39-46
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• 1999

As a preliminary study for the explanation of pathobiology of Neodiplostomum seoulense infection. a 54 kDa protease was purified from the crude extract of adult worms by sequential chromatographic methods. The crude extract was subjected to DEAE-Sepharose Fast Flow column, and protein was eluted using 25 mM Tris-HC1 (pH 7.4) containing 0.05. 0.1, 0.2 and 0.4 M NaC1 in stepwise elution. The 0.2 M NaCl fraction was further purified by Q-Sepharose chromatography and protein was eluted using 20 mM sodium acetate (pH 6.4) containing 0.05, 0.1. 0.2 and 0.3 M NaCl, respectively. The 0.1M NaCl fraction showed a single protein band on SDS-PAGE carried out on a 7.5-15% gradient gel. The proteolytic activities of the purified enzyme were specifically inhibited by L-trans-epoxy-succinylleucylamide (4-guanidino) butane (E-64) and iodoacetic acid. The enzyme, cysteine protease. showed the maximum proteolytic activity at pH 6.0 in 0.1 M buffer, and degraded extracellular matrix proteins such as collagen and fibronectin with different activities. It is suggested that the cysteine protease may playa role in the nutrient uptake of N. seoulense from the host intestine.