• 한국생물공학회:학술대회논문집
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• 2003.10a
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• pp.544-547
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• 2003

Fusion $ferritin(F_H+F_L),$ an iron-binding protein, was purified from recombinant E. coli by gel filtration chromatography after two-step sonications. Unfolded ferritin was refolded by GFC with various refolding enhancing additives. 50 mM Tris-HCI(pH 7.4) buffers containing 2 M urea and additive was used in GFC. Objective was to characterize the structure change at various conditions. Molecular weight was determined using GF-HPLC and RP-HPLC was used to quantify the unfolded and refolded proteins. Activity was confirmed by iron-uptake reaction.

• Preventive Nutrition and Food Science
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• v.5 no.3
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• pp.148-152
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• 2000

Mussel adhesive protein (MAP) was extracted from Korean Mytilus edulis and then partially purified using Sephacryl S-300 gel permeation chromatography and reversed-phase high performance liquid chromatography. As an indicator of adhesiveness, is 3,4-dihydroxyphenylalanine (DOPA) content was determined. Its DOPA/protein ratio of 0.19 was higher than those of other reports, indicating a good adhesive. The partially purified MAP was confirmed by acid-urea polyacrylamide gel electrophoresis using cetylpiridinium bromide as a cationic detergent. Sea mussel hydrolysates were prepared using three commercial proteases to provide value-added functional materials and their angiotensin converting enzyme (ACE) inhibitory activities were determined. Among hydrolysates of sea mussel, Protamex was the best and further purification would improved ACE inhibitory activity.

• Journal of the Korean Society of Food Science and Nutrition
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• v.19 no.4
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• pp.335-341
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• 1990

Nuclei proteins were purified from chick liver to homogeneity by means of acid extraction CM Sephadex c 25 column chromatography and Bio Rex 70 column chromatography, The molecular weight of liver Nuclei proteins 1 and 2 as estimated by electrophoresis on SDS-polycrylamide gel are 29000 and 27,000 respectively. These molecular weights are identical with those of Nuclei Proteins 1 and 2 isolated from chick erythrocyte. The liver and erythrocyte Nuclei Proteins also co-migrated in acetic acid-urea gel electrophoresis. Furthermore the anti-sera raised against liver Nuclei Proteins 1 and 2 cross-reacted with erythrocyte Nuclei Proteins 1 and 2 respectively, However the amino acid compositions of liver Nuclei Prooteins 1 and 2 were found to be different from those of corresponding erythrocyte Nuclei proteins ; the contents of serine and proline in liver Nuclei proteins were higherocyte Nuclei proteins ; the contents of serine and proline in liver Nuclei protesins were higher than those in erythrocyte Nuclei proteins while the content of lycsine in liver Nuclei proteins was lower than the erythrocyte Nuclei proteins, These results suggest that in spite of similarities in many respects the liver and erythrocyte Nuclei proteins in chicks and different proteins.

• KSBB Journal
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• v.11 no.4
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• pp.453-461
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• 1996

We compared the effects of two different systems of collagen matrix protein application on the survival and the biological functions of cultured primary hepatocytes. The rat liver primary hepatocytes were grown for approximately 40 days in vitro either on single collagen gel or between collagen sandwich gels. The morphological changes were observed for this culture period. While the hepatocytes grown on single gel began to die around at 7 days of culture, the cells grown between collagen gels still maintained their viability and began to die after 15 days. As markers for liver hepatic functions, we determined the biochemical activities of hepatocytes such as the secretions of albumin, fibronectin, fibrinogen, urea, and the reduction of secreted ammonia. We found that the rat hepatocytes cultured between collagen gels maintained fairly good biochemical functions than the hepatocytes cultured on single gel did. Therefore, the application of an extracellular matrix protein, collagen, in sandwich form was confirmed as a better choice for maintaining the functional hepatocytes culture for long term in vitro.

• Asian Journal of Turfgrass Science
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• v.4 no.1
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• pp.12-23
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• 1990

The chlorophyll-protein complexes were separated from thylakoid membranes of Spinach oleracea and Zoysia japonica by two gel Systems of LiDodSO4-PAGE and LiDodSo4/Urea- PAGE under nondenaturing conditions. Seven chlorophyll~protein complexes of CPI*, CPI, CPII*. CP47, CP43, CP29 and CPII were fractionated from both S,oleracea and Zjaponica by LiDodSO4-PAGE. CPI, CP47 and CP43 contained more chlorophyll a than chlorophyll b. The patterns of their absorption spectra at room temperature were similliar to that of chlorophyll a, judging by their UV-spedtroscopy. On the other hand, CPII* and CPII contained approximately equim-olar quantities of chlorophyll a and b. Additional five chlorophyll-protein complexes not separated in the LiDodSO4-PAGE system were electrophoretically isolated from both S, oleracea and Zjaponica by LiDodSO4/Urca-PAGE. The chlorophyll-protein complex just above LRCII $\alpha$in the gel appears CCII-RC separeted recently. 23 kDa and 20 kDa cho-protein complexes is probably LHCIa and LHCIb as judged from their molecular weight. Two novel chlorophyll~protein complexes designated "CPI7" and "CPI6" were fractionate by this gel system. Their molecular weights respectively. Although the stoichiometry of their components and their roles in thylakoid membranes are not apparant, It is thought that they are another kinds of LHCI.other kinds of LHCI.

• The Journal of the Korean Society for Microbiology
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• v.35 no.2
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• pp.97-108
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• 2000

Two-dimensional gel electrophoresis (2-DE) is an essential tool of proteomics to analyse the entire set of proteins of an organism and its variation between organisms. Helicobacter pylori was tried to identify differences between strains. As the first step, whole H. pylori was lysed using high concentration urea contained lysis buffer [9.5 M Urea, 4% CHAPS, 35 mM Tris, 65 mM DTT, 0.01% SDS and 0.5% Ampholite (Bio-Rad, pH 3-10)]. The extract ($10\;{\mu}g$) was rehydrated to commercially available immobilised pH gradient (IPG) strips, then the proteins were separated according to their charges as the first dimensional separation. The IPG strips were placed on Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE) to separate according to molecular mass of the proteins as the second dimension. The separated protein spots were visualised by silver staining in order to compare different expression of proteins between strains. Approximately 120 spots were identified in each mini-protein electrophoresised gel, furthermore about 65 to 75 spots were regarded as identical proteins in terms of pI value and molecular weight between strains used. In addition, distinct differences were found between strains, such as 219-1, Y7 and Y14, CH150. Two representative strains were examined using strips which had pH range from 4 to 7. This strips showed a number of isoforms which were considered large spots on pH range 3-10. Furthermore, the rest of spots on pH 4-7 IPG strips appeared very distinctive compared to broad range IPG strips. 2-DE seems to be an excellent tool for analysing and identifying variations between H. pylori strains.

• Clean Technology
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• v.22 no.4
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• pp.258-268
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• 2016

In this work, carboxymethylcellulose-based composite superabsorbent hydrogels were prepared by electron beam radiation. The composition of carboxymethylcellulose (CMC) varied from 4 wt%, 5 wt%, and 6 wt% to 7 wt% based on the amount of distilled water in the syntheses of hydrogels. Graphite oxide, reduced graphene oxide, activated carbon, and bentonite were used as additives for the synthesis of composite superabsorbent. The effect of CMC composition and the type of additives on the gel properties of the prepared hydrogels was investigated. In order to verify the functional groups in the prepared materials, Fourier transform infrared spectroscopy was used. In addition, mechanical strength, gel fraction, swelling kinetics, and equilibrium swelling ratios were measured for the prepared hydrogels. Swelling experiments were carried out in distilled water, urea solution, and physiological saline water. Prepared hydrogels were reused for 5 times, and gel fraction and swelling ratio were measured at every 24 hours. Among the prepared hydrogels, $C_{5%}GO$ and $C_{5%}rGO$ exhibited excellent mechanical property and relatively high swelling ratios for urea solution and physiological saline water with promising applicability as slow-release fertilizers.

• Journal of Microbiology and Biotechnology
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• v.16 no.2
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• pp.286-290
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• 2006

A genomic library of Streptococcus vestibularis ATCC49124 was constructed in an E. coli plasmid vector, and the urease-positive transformants harboring the urease gene cluster were isolated on Christensen-urea agar plates. The minimal DNA region required for urease activity was located in a 5.6 kb DNA fragment, and a DNA sequence analysis revealed the presence of a partial ureI gene and seven complete open reading frames, corresponding to ureA, B, C, E, F, G, and D, respectively. The nucleotide sequence over the entire ure gene cluster and 3'-end flanking region of S. vestibularis was up to 95% identical to that of S. salivarius, another closely related oral bacterium, and S. thermophilus, isolated from dairy products. The predicted amino acid sequences for the structural peptides were 98-100% identical to the corresponding peptides in S. salivarius and S. thermophilus, respectively, whereas those for the accessory proteins were 96-100% identical. The recombinant E. coli strain containing the S. vestibularis ure gene cluster expressed a high level of the functional urease holoenzyme when grown in a medium supplemented with 1 mM nickel chloride. The enzyme was purified over 49-fold by using DEAE-Sepharose FF, Superdex HR 200, and Mono-Q HR 5/5 column chromatography. The specific activity of the purified enzyme was 2,019 U/mg, and the Michaelis constant ($K_{m}$) of the enzyme was estimated to be 1.4 mM urea. A Superose 6HR gel filtration chromatography study demonstrated that the native molecular weight was about 196 kDa.

• Journal of Korea Technical Association of The Pulp and Paper Industry
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• v.47 no.6
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• pp.113-122
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• 2015

This study was carried out to investigate the characterization of cadmium adsorption by cellulose hydrogel and aerogel. Hydrogel and aerogel were made from ashless pulp dissolved in alkali hydroxide-urea aqueous solution and manufactured in film and bead types. After regeneration of cellulose, hydrogel went through the process of substitution of organic solvent and freeze-dry in order to make aerogel. SEM was used to analyze the microstructure of hydrogel and aerogel. Experiment was conducted in various concentrations and pH conditions to find out the characteristic of cadmium adsorption. After that, EDS was used to identify existence and distribution of cadmium in hydrogel and aerogel. The result from comparisons of cadmium adsorption shows that bead type aerogel has the maximum cadmium adsorption and film type hydrogel has the minimum cadmium adsorption.

• Journal of the Korean Society of Food Science and Nutrition
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• v.23 no.2
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• pp.308-314
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• 1994

Four Taro isolectins (I, II, III, IV) were purified by ammonium sulfate, chromatography on CM-celluose and isoelectric focusing. I and IV lectins proved homogeneous by disk polyacrylamid gel electrophoresis and densitometric patterns. But in the presence of urea, IV lectin further dissociated into two different subunits. These lectinis had different hemagglutinating activities and inhibition in their activities after mixed with pepsin particuclary, but not with carbohydrates, heating pH, urea, guanidine, trypsin, pronase and $Ca^{2+}$.