• Bulletin of the Korean Chemical Society
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• 제30권4호
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• pp.955-958
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• 2009

• 폴리머
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• 제33권5호
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• pp.420-428
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• 2009

In this study, the composites containing carbon black (CB) or carbon fibers were prepared, and the microwave absorbing properties and the absorption mechanism of them were investigated and discussed in the frequency range of 2-18 GHz, respectively. The optimum mass fraction of CB has been found as 6%, and the carbon fibers were discovered to absorb radar wave either under parallel or vertical polarization, the suitable gap distance between each bundle of which was 5 mm. According to the results of the single constitute absorber samples, the structured composites with the two kinds of absorbers combination were fabricated and studied at 2-18 GHz. The top layer absorbers affect the absorption performance a lot; the maximum reflection loss of composites with CB as top layer absorbers was -31.8 dB with the frequency range of 2.4 GHz below -10 dB, and the other type with CFs as the top layer absorbers obtained the reflection loss peak value of -31.4 dB with 2 GHz below-10 dB.

• BMB Reports
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• 제28권2호
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• pp.124-128
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• 1995

Biodegradative threonine dehydratase purified from Serratia marcescens ATCC 25419 was inactivated by the arginine specific modification reagent, phenylglyoxal (PGO) and the lysine modification reagent, pyridoxal 5'-phosphate (PLP). The inactivation by PGO was protected by L-threonine and L-serine. The second order rate constant for the inactivation of the enzyme by PGO was calculated to be 136 $M^{-1}min^{-1}$. The reaction order with respect to PGO was 0.83. The inactivation of the enzyme by PGO was reversed upon addition of excess hydroxylamine. The inactivation of the enzyme by PLP was protected by L-threonine, L-serine, and a-aminobutyrate. The second order rate constant for the inactivation of the enzyme by PLP was 157 $M^{-1}min^{-1}$ and the order of reaction with respect to PLP was 1.0. The inactivation of the enzyme by PLP was reversed upon addition of excess acetic anhydride. Other chemical modification reagents such as N-ethylmaleimide, 5,5'-dithiobis (2-nitrobenzoate), iodoacetamide, sodium azide, phenylmethyl sulfonylfluoride and diethylpyrocarbonate had no effect on the enzyme activity. These results suggest that essential arginine and lysine residues may be located at or near the active site.

• Bulletin of the Korean Chemical Society
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• 제32권7호
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• pp.2351-2357
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• 2011

Three new metal-organic copper(II) complexes, $[Cu(H_2PZTC)_2]_n{\cdot}2nH_2O$ (1), $[Cu(HPZTC){\cdot}2H_2O]_n{\cdot}2nH_2O$ (2), and $Cu_2[(PZHD)(OH)(H_2O)_2]_n$ (3) ($H_3PZTC$ = pyrazine-2,3,5-tricarboxylic acid, $PZHD^{3-}$ = 2-hydroxypyrazine-3,5-dicarboxylate), have been synthesized from $Cu(II)/H_3PZTC$ system under different synthetic conditions, and characterized by single-crystal X-ray diffraction, elemental analysis, IR spectroscopy and thermogravimetric analysis. In complexes 1 and 2, $H_3PZTC$ ligands loose one and two protons, which were transformed into $H_2PZTC^-$ anion and $HPZTC^{2-}$ dianion under different preparation condition, respectively. Furthermore, two ligands coordinate with Cu(II) cations in different modes, leading to the formation of the different chain structures. In complex 3, $H_3PZTC$ ligand was converted into a new ligand-PZHD by in situ decarboxylation and hydroxylation under a higher pH value than that for complexes 1 and 2. PZHD ligands link the Cu(II) cations to form a 2D layer structure. These results demonstrate that the preparation conditions, including pH value and reaction temperature etc, play an important role in the construction of complexes based on $H_3PZTC$ ligand.

• Bulletin of the Korean Chemical Society
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• 제27권4호
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• pp.529-534
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• 2006

Chemical modification of the S. cerevisiae farnesyl protein transferase (FPT) with CMC, phenylglyoxal and DEPC resulted in enzyme inactivation, depending upon the reagent concentration. The peptide substrate GST-PEP-I, a GST-fused undecapeptide mimicking the C-terminus of $p21^{Ki-ras}$, protected the enzyme against inactivation by CMC which is specific to either aspartate or glutamate, while the other substrate farnesyl pyrophosphate (FPP) showed protection against phenylglyoxal which is the specific modifier of arginine residues, dependent on the substrate concentrations. Neither of the two substrates protected the enzyme against histidine inactivation by DEPC. It is suggested that there is at least one aspartate or glutamate residue at the peptide substrate binding site, and that at least one arginine residue is located at the binding site of FPP. There also seems to be at least one histidine residue which is critical for enzymic activity and is exposed toward the bulk solution, excluded from the substrate binding sites.

• Bulletin of the Korean Chemical Society
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• 제28권1호
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• pp.118-120
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• 2007

• 상하수도학회지
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• 제34권6호
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• pp.425-435
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• 2020

Numerous chemical modifications on activated carbon such as acidic conditioning, thermal treatment and metal impregnation have been investigated to enhance adsorption capacities of micropollutants in water treatment plants. In this study, chemical modification including acidic, alkaline treatment, and iron-impregnation was evaluated for adsorption of 2,4-dichlorophenol (2,4-DCP). For Fe-impregnation, three concentrations of ferric chloride solutions, i.e., 0.2 M, 0.4 M, and 0.8 M, were used and ion-exchange (MIX) of iron and subsequent thermal treatment (MTH) were also applied. Surface properties of the modified carbons were analyzed by active surface area, pore volume, three-dimensional images, and chemical characteristics. The acidic and alkaline treatment changed the pore structures but yielded little improvement of adsorption capacities. As Fe concentrations were increased during impregnation, the active adsorption areas were decreased and the compositional ratios of Fe were increased. Adsorption capacities of modified ACs were evaluated using Langmuir isotherm. The MIX modification was not efficient to enhance 2,4-DCP adsorption and the MES treatment showed increases in adsorption capacities of 2,4-DCP, compared to the original activated carbon. These results implied a possibility of chemical impregnation modification for improvement of adsorption of 2,4-DCP, if a proper modification procedure is sought.

• BMB Reports
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• 제37권6호
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• pp.642-647
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• 2004

The lysine residues of Bacillus licheniformis $\alpha$-amylase (BLA) were chemically modified using citraconic anhydride or succinic anhydride. Modification caused fundamental changes in the enzymes specificity, as indicated by a dramatic increase in maltosidase and a reduction in amylase activity. These changes in substrate specificity were found to coincide with a change in the cleavage pattern of the substrates and with a conversion of the native endo- form of the enzyme to a modified exo- form. Progressive increases in the productions of $\rho$-nitrophenol or glucose, when para nitrophenyl-maltoheptaoside or soluble starch, respectively, was used as substrate, were observed upon modification. The described changes were affected by the size of incorporated modified reagent: citraconic anhydride was more effective than succinic anhydride. Reasons for the observed changes are discussed and reasons for the effectivenesses of chemical modifications for tailoring enzyme specificities are suggested.

• Preventive Nutrition and Food Science
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• 제2권1호
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• pp.17-22
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• 1997

Casein was chemically modified with acetic, succinic, and maleic anhydride and changes in functional pro-perties were evaluated as affected by the degree of modification. Chemical modification resulted in casein with unique functional properties depending upon the type of anhydrid used and the degree of modification. It was possible to control heat coagulation, calcium precipitability, forming and emulsion capacity and stability. At pH 4.5 heat coagulation was 0% in the case 74.1% acetylated casein; on the contrary, succinylation and maleyation resulted in highly heat sensitive protein. Foaming properties were improved markedly by suc-cinylation and maleylation at pH 4.5. However, emulsifying properties were enhanced only by maleylation.

• Journal of Microbiology and Biotechnology
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• 제5권3호
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• pp.163-166
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• 1995

Chemical modification of gelatin-based macroporous microcanier beads was achieved by increasing the charge density through incorporation of (diethylamino)ethylchloride-hydrochloride (DEAE:CI-HCI) or lysine, and this significantly improved the attachment and growth of HepG2 cells. When microcarriers were modified by the addition of 2% lysine, positive charge density was 0.95 meq/g-caniers. In case of modification of microcarriers with DEAE:CI-HCI, positive charge density was 0.6 meq/g-caniers. An increase in charge density of the microcaniers to improve cell attachment has facilitated the growth of the cells on macroporous gelatin microcaniers. Also, final HepG2 cell concentration cultivated on modified beads with DEAE:CI-HCI was increased up to $10^7$ cells/ml. This was 2-3 times higher than that obtained with unmodified macroporous gelatin microcarriers.