• Applied Chemistry for Engineering
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• v.4 no.3
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• pp.616-626
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• 1993

Polyurethane(PU) have an excellent flexibility and toughness so that it has been widely used as an elastomer. PMMA was blended with PU to improve the impact property. Five types of PU, having different molecular weight and different polyol types, were prepared and blended with PMMA in order to investigate the effect of molecular weight and polyol type of PU on property of PU-PMMA blend. Tensile strength of PU-PMMA blend was determined by Inston. Differential Scanning Calorymetry(DSC) and Scanning. Elctron Microscopy(SEM) were used to observe morphology change and glass transition temperature changes of PU-PMMA blends. Transparency of PU-PMMA blends was determined by haze meter. But, owing to intrinsic incompatability of PU-PMMA, Low impact strength of PMMA wasn't improved through PU-PMMA blend. therefore, polyurethane dimethacrylate(PUD), having similiar chemical structure to PU and two vinyl group at both ends, was prepared and reacted with methyl methacrylate(MMA) to form crosslinked copolymer Mechanical property of this crosslinked polymer, such as impact strength and transparency, was investigated by Instron, Izod type (Cantilever beam) impact tester and haze meter. Results of these measurements showed that crosslinked copolymer of PUD-MMA was better impact resistance than PMMA and maintained similar transparency to PMMA.

• The Korean Journal of Mycology
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• v.17 no.3
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• pp.105-113
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• 1989

For selective purification of proteins in Pleurotus cornucopiae, affinity chromatography was performed by p-aminoanilinylsuccinyl-AH-Sepharose 4B gel synthesized by treating p-phenylene diamine with succinyl-AH-Sepharose 4B, which was prepared by treating AH-Sepharose 4B with succinic anhydride. The capacity of p-aminoanilinyl ligand group was 6.1 micromole per milliliter of gel. Total apparent molecular weight of the affinity proteins eluted from the synthesized gel was 167 KD, which were a protein complex of 130 KD and 37 KD. The contents of the nonpolar, polar, positively and/or negatively charged amino acids in the affinity protein were 44.57%, 24.75%, 21.25%, and 9.43%, respectively. Total apparent molecular weight of the affinity proteins eluted from the AH-Sepharose 4B gel was 95.2 KD, which were a protein complex of 61 KD, 31 KD and 3.2 KD. The contents of the nonpolar, positively and/or negatively charged amino acids in the affinity protein by AH-Sepharose 4B gel were 44.05%, 29.13%, and 12.91% respectively.

• KSBB Journal
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• v.21 no.2
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• pp.133-139
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• 2006

In 'solid-phase' PEGylation, the conjugation reaction occurs as the proteins are attached to a solid matrix, and thus it can have distinct advantages over the conventional, solution-phase process. We report a case study: rhIFN-${\alpha}$-2a was first adsorbed to cation exchange resin and then N-terminally PEGylated by aldehyde mPEG of 5, 10, and 20 kD through reductive alkylation. After the PEGylation, salt gradient elution efficiently recovered the mono-PEGylate in a purified form from the unwanted species such as unmodified IFN, unreacted PEG, and others. The mono-PEGylation and its purification were integrated in a single chromatographic step. Depending on the molecular weight of the mPEG aldehyde used, the mono-PEGylation yield ranged 50-64%. We could overcome the major problems of random, or uncontrollable, multi-PEGylation and the post-PEGylation purification difficulties associated with the solution-phase process. N-terminal sequencing and MALDI-TOF MS confirmed that a PEG molecule was conjugated only to the N-terminus. Compared with the unmodified IFN, the mono-PEGylate showed the reduced anti-viral activity as measured by the cell proliferation assay. The bioactivity was reduced more as the higher molecular weight PEG was conjugated. Immunoreactivity, evaluated indirectly by antibody binding activity using a surface plasmon resonance biosensor, also decreased. Nevertheless, trypsin resistance as well as thermal stability was considerably improved.

• Applied Chemistry for Engineering
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• v.3 no.4
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• pp.595-604
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• 1992

Carbonate-type polyurethane resins containing anionic moieties were systhesized from NCO-terminated prepolymer method. Membranes were manufactured from the polymer solution and the separation of aqueous ethanol solution was investigated. To enhance the property of urethane resin, carbonate-type polyol(PTMCG) was used. ${\alpha}^{\prime},{\alpha}^{{\prime}{\prime}}$-dimethylolpropionic acid was used as a chain extender to increase the hydrophilicily of the urethane membrane. The ionization of the pendent carboxylic groups in urethane resin was carried out using trimthylamine. To confirm the formation of anionic groups in urethane resin, IR spectra of model compounds were compared with those of urethane resins. It was confirmed that the concentration of hard segment and hydrogen bond contributed to the property of the concentration of hard segment and hydrogen bond contributed to the property of urethane resin in which the mole ratio of chain extender and polyol was from 3:1 to urethane resin in which the mole ratio of chain extender and polyol was from 3:1 to 5:1. The carbonate-type polyurethane containing pendent carboxylic grop(PU) had Tg of around-$25^{\circ}C$ and Tm, $45^{\circ}C$ measured by DSC. Transition temperatures of one containing pendent anionic group(APU) prepared from the ionization of PU shifted to $8{\sim}10^{\circ}C$ lower temperature region than those of PU. Pervaporation membrane was prepared through the casting method. N, N-dimethylformamide (DMF) were used as a solvent and hexamethylene diisocyanate(HMDl) as a crosslinking agent. Swelling degree increased with ethanol concentration in mixure and the control of the swelling degree of the membrane could be achieved by crossliking. The results of pervaporation were as follows : separation factor, 2.3~9.8 ; flux, $27{\sim}79.5g/m^2hr$. Pervaporation separation capacity could be enhanced by reducing the molecular weight of polyol from 2,000 to 1,000.

• Applied Chemistry for Engineering
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• v.20 no.3
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• pp.339-345
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• 2009

The graft copolymerization of acrylonitrile-EPDM-styrene (AES) was investigated under various reaction conditions such as the concentration of initiator, the content of diene and viscosity of EPDM, and the concentration of solvents. The conversion increased but the molecular weight and the rubber particle size decreased with the concentration of initiator. The graft ratio(GR) increased at low concentrations of the initiator but, after the maximum value, it gradually decreased with the concentration of initiator. Toluene as a single solvent gave the highest conversion and the mixture of ethyl benzene and toluene was better than toluene. The rubber particle size increased with the viscosity of EPDM and the graft ratio and the number of rubber particles with occluded SANs increased with the content of diene.

• Journal of Applied Biological Chemistry
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• v.52 no.3
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• pp.109-115
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• 2009

The gene encoding a putative aspartate aminotransferase in Xanthomonas oryzae pv. oryzae (Xoo) was cloned using PCR technique. The gene was ligated with pET-21(a) vector containing His6 tag and expressed in E. coli BL21(DE3). Affinity purification of the recombinant aspartate aminotransferase with Ni-NTA resin resulted in one band by SDS-PAGE analysis. The purified enzyme showed a molecular weight of 43 kDa, as expected. The enzyme was the most active toward L-aspartate as an amino donor, indicating that the purified enzyme is one of aspartate aminotrans-ferases exist in Xoo. Optimal activity of the enzyme was observed at around pH 7.5 and stability was much higher at alkaline pH rather than acidic pH values. The enzyme was considerably activated by the presence of manganese ion, showing about 157% of control activity at 1.0 mM.

• 한국생물공학회:학술대회논문집
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• 2003.04a
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• pp.334-338
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• 2003

In this study, We evaluated the removal efficiency of natural organic matters(NOM) in the Ultrafiltration(UF) and Nanofiltration(NF) membranes with molecular weight cutoff of 2500(GH), 8000(GM) and 250(HL), respectively. Filtration type was cross-flow filtration. The investigation result about raw water structure was hydrophobic 28%, hydrophilic 53% and transphilic 19%, in conjunction with XAD8/4 resin fractionation method. We were compared with UF(GM, GH) and NF(HL), in operation characteristic. In spite of poor MWCO, GM(8000Da) was superior than GH(2500Da), in the efficiency of total operation. It was showed the NF(HL) 80%, UF(GM) 50%, in the removing efficiency of HAAFP.

• Applied Chemistry for Engineering
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• v.9 no.1
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• pp.66-70
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• 1998

Several liquid crystalline monomers were synthesized and characterized to utilize as new matrix materials of liquid crystal/polymer composite films for display application. Liquid crystalline compounds which have azo group as center link, cyano group at one of the terminal position in common and bromoalkyl(azo(n)), azidoalkyl(AZI(n)), aminoalkyl(ALC(n)) as the terminal group were synthesized and identified respectively by FT-lR, $^1H-NMR$ spectrometer and elemental analysis. All these compounds exhibited nematic liquid crystalline region in the certain temperature range as determined by DSC and polarized optical microscope. These liquid crystalline compounds also showed a typical even-odd effect in both $T_{KN}$ and $T_{NI}$ due to conformational change as the length of terminal alkyl chain, $-(CH_2)n-$. was varied.

• Journal of Applied Biological Chemistry
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• v.53 no.3
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• pp.132-138
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• 2010

A gene encoding a putative alanine racemase in B. pseudomycoides was cloned and expressed in Escherichia coli BL21(DE3) using a pET-21 vector harbouring 6xHistidine tag. Affinity purification of the recombinant alanine racemase with a nickel resin resulted in one band by SDS-PAGE analysis. The purified enzyme showed a molecular weight of 46 kDa. The enzyme was the most active toward L-alanine and secondly D-alanine, implying that the enzyme is an alanine racemase. D-cysteine significantly inhibited the enzyme activity and also L-cysteine to a lesser extent. The enzyme was considerably activated by addition of pyridoxal-5'-phosphate (PLP), showing that 73% increase in activity was observed at 0.3 mM, compared to control. The enzyme was the most active at pH 9.0 and more stable at alkaline pHs than acidic pHs.

• Microbiology and Biotechnology Letters
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• v.31 no.3
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• pp.224-229
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• 2003

A keratinolytic protease was purified from the culture medium of Pseudomonas sp. KP-364 by use of an assay of the hydrolysis of feather keratin. Membrane ultrafiltration and DEAE-cellulose ion-exchange resin and Sephadex G-150 gel chromatographies were used to purify the enzyme. The specific activity of the purified keratinolytic protease relative to that in the original medium was approximately 72-fold high. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Sephadex G-150 chromatography indicated that the purified keratinolytic protease is monomeric and has a molecular weight of 36 kDa. The optimal pH and temperature of the keratinolytic protease activity were 6.6 and 37 C, respectively, and the keratinolytic protease was relatively stable at pH value from 3.0 to 10.0 at 37 C for 1hour. The keratinolytic protease was inhibited by EDTA and EGTA, indicating that the keratinolytic protease was a kind of metalloprotease that require Li+ for cofactor.