• Journal of the Korean Vacuum Society
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• v.19 no.2
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• pp.81-90
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• 2010

We introduce a novel and versatile approach for preparing self-assembled nanoporous multilayered films with antireflective properties. Protonated polystyrene-block-poly (4-vinylpyrine) (PS-b-P4VP) and anionic polystyrene-block-poly (acrylic acid) (PS-b-PAA) block copolymer micelles (BCM) were used as building blocks for the layer-by-layer assembly of BCM multilayer films. BCM film growth is governed by electrostatic and hydrogen-bonding interactions between the oppositely BCMs. Both film porosity and film thickness are dependent upon the charge density of the micelles, with the porosity of the film controlled by the solution pH and the molecular weight (Mw) of the constituents. PS7K-b-P4VP28K/PS2K-b-PAA8K films prepared at pH 4 (for PS7K-b-P4VP28K) and pH 6 (for PS2K-b-PAA8K) are highly nanoporous and antireflective. In contrast, PS7K-b-P4VP28K/PS2K-b-PAA8K films assembled at pH 4/4 show a relatively dense surface morphology due to the decreased charge density of PS2K-b-PAA8K. Films formed from BCMs with increased PS block and decreased hydrophilic block (P4VP or PAA) size (e.g., PS36K-b-P4VP12K/PS16K-b-PAA4K at pH 4/4) were also nanoporous. Furthermore, we demonstrate that the nanostructured electrochemical sensors based on patterning methods show the electrochemical activities. Anionic poly(styrene sulfonate) (PSS) layers were selectively and uniformly deposited onto the catalase (CAT)-coated surface using the micro-contact printing method. The pH-induced charge reversal of catalase can provide the selective deposition of consecutive PE multilayers onto patterned PSS layers by causing the electrostatic repulsion between next PE layer and catalase. Based on this patterning method, the hybrid patterned multilayers composed of platinum nanoparticles (PtNP) and catalase were prepared and then their electrochemical properties were investigated from sensing $H_2O_2$ and NO gas. This study was based on the papers reported by our group. (J. Am. Chem. Soc. 128, 9935 (2006); Adv. Mater. 19, 4364 (2007); Electro. Mater. Lett. 3, 163 (2007)).

• Archives of Pharmacal Research
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• v.19 no.2
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• pp.116-121
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• 1996

Antisense oligonucleotides seem to provide a promising new tool for the therapy. Choi et al. (1995) reported antisense phosphorothioate oligonucleotides (PS-ODN, 25 mer) complementary to TGF-.betha. mRNA designed for scar formation inhibitor to eliminate scars, which was caused by undesired collagen deposition due to overexpression of TGF-.betha., in wounded skin. PS-ODN were evaluated in vitro for skin penetration using normal and tape-stripped damaged rat skin. The in vitro skin transports were carried out with partially modified PS-ODN (6S) and fully modified PS-ODN (25S). The cumulative amount of PS-ODN (6S) penetrated through normal rat skin was $0.234{\pm}0.041{\mu}g/cm^2$ and that of tape-stripped damaged rat skin was $1.077{\pm}0.301{\mu}g/cm^2$ over 8 hrs. PS-ODN (25S) can not be found in receptor medium through normal skin due to high molecular weight (Mol.Wt.=8,000) and polyanionic charge. However, the cumulative amount of PS-ODN (25S) penetrated across damaged rat skin in PBS was $0.340{\pm}0.296{\mu}g/cm^2$ over 8 hrs. The absense of dermis raised the cumulative amount of PS-ODN (6S) penetrated through rat skin. And the fluxes of PS-ODN (6S) and PSODN (25S) at 8hrs across damaged rat skin were $134.63{\pm}37.67{\mu}g/cm^2$ h, and $42.50{\pm}36.95ng/cm^2$ h, respectively. While PS-ODN (25S) was stable in 10% heat inactivated fetal bovine serum (FBS) during 24 hrs, PS-ODN (6S) was less stable than PS-ODN (25S), but was markedly stable than unmodified phosphodiester. It is suggested that the cumulative amount of PS-ODN (6S) penetrated through damaged rat skin is larger than that of PS-ODN (25S) since the former is easier to degrade by nuclease than the latter and then is apt to penetrate into skin. Thus, PS-ODN represents a logical candidate for further evaluation due to the potential for delivery into the wounded skin.

• Korean Journal of Food Science and Technology
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• v.37 no.5
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• pp.695-701
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• 2005

Efficient method was established for analysis of sulfur-containing compounds, including dimethyl disulfide, dimethyl trisulfide, 3-methyl thiophene, allyl mercaptan, 2-methyl-3-furanthiol, and methional. Sulfur-containing compounds were extracted through solid phase microextraction (SPME) or static headspace extraction (SH), and quantified using gas chromatograph equipped with pulsed flame photometric detector. All sulfur compounds, except ally mercaptan, showed higher detection response when dissolved in hexane than in dichloromethane. Linear range was $10^2-10^4$. Dimethyl trisulfide showed lowest limit of detection (LOD) value of 15.2 ppt, and methional highest of 70.5 ppb. Highest extraction efficiency for sulfur-containing compounds, particularly polar and small molecular weight compounds, was observed in 75mm carboxen/polydimethylsiloxane fiber, followed by 65mm polydimethylsiloxane/divinylbenzene and 100mm polydimethylsiloxane. Compared to SPME, less sulfur-containing compounds could be analyzed by SH, mainly due to its low extraction efficiency, although lower amount of artifacts were formed during sample preparation.

• Korean Journal of Food Science and Technology
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• v.32 no.1
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• pp.161-167
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• 2000

The protease produced by a newly isolated Aspergillus wentti from Korean traditional Meju was purified and characterized. The optimal medium composition and culture conditions for maximum protease production were ; bran :1% glucose solution =1 : 1, pH 9.0, $30^{\circ}C$, and 4 days of fermentation. Protease was purified by QAE-Sephadex, SP-Sephadex ion exchange chromatography and Sephadex G-100 chromatography. The specific activity and the purification fold of the purified enzyme were 213 unit/mg protein and 27.3, respectively. The molecular weight of purified protease was found to be 32 kDa by SDS-PAGE. Km and Vmax value's for hammastein milk casein were $3.049{\times}10^{-4}\;M\;and\;151.1\;{\mu}g/min$, respectively. Kinetic parameters showed that the enzyme has higher affinity to casein than isolated soybean protein, hemoglobin and bovine serum albumin. Optimal pH and temperature for reaction of the purified enzyme were 9.0 and $50^{\circ}C$, respectively. The enzyme was stable at pH 4.0-11.0, below $40^{\circ}C$, and the activity was not stimulated by metal ions. 1mM phenylmethylsulfonyl fluoride inhibited the enzyme activity by 98.5%. It means that the enzyme is one of serine protease.

• Korean Journal of Food Science and Technology
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• v.16 no.2
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• pp.228-234
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• 1984

A partial hydrolysis of soybean protein isolate was carried out by using pepsin and trypsin. The degree of hydrolysis was evaluated by chemical analysis, viscometric measurements and gel electrophoresis. The functional properties of the hydrolyzates such as flow behavior, emulsion properties and foaming properties were evaluated. A selective hydrolysis of 11S protein fraction by pepsin was observed from the SDS-PAG electrophoresis. The changes in the molecular weight distribution by different conditions of enzyme hydrolysis were evaluated. The changes in the intrinsic viscosity of the protein hydrolylate by reaction time were highly correlated to the contents of TCA soluble protein and 0.03 M $CaCl_2$ soluble nitrogen. The degree of hydrolysis ($DH_{TCA}$, $DH_{Ca}$) were used to evaluate the effect of enzyme treatment on the functional properties of the hydrolyzate. The apparent viscosity and emulsion capacity and stability of the protein solution decreased as DH increased, while the foaming capacity increased linearly with the increasing DH.

• Korean Journal of Food Science and Technology
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• v.19 no.1
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• pp.29-37
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• 1987

The native myosin and paramyosin extracted from the ordinary muscle of yellowtail (Seriola quinqueradita) and the adductor muscle of whelk (Neptunea arthritica cumingi) were studied for their physico-chemical characteristics. Molecular weight, molar extinction coefficient at 278 nm and intrinsic viscosity were accounted for $4.6{\times}10^5$dalton, 5.44 in $E^{1cm}_{1%}$ and 1.60 dl/g in yellowtail myosin, and $2.0{\times}10^5$ dalton, 3.04 in $E^{1cm}_{1%}$ and 2.60 dl/g in whelk paramyosin, respectively. Yellowtail myosin showed a $0.342\;{\mu}mole-Pi/min/mg-protein$ of ${Ca}^{2+}-ATPase$ activity and contained 40 group-SH/mole-myosin. The ratio of polar amino acids to non-polar amino acids and that of acidic amino acids to basic amino acids were 0.54 and 1.64 in yellowtail moysin, and were 0.47 and 2.42 in whelk paramyosin, respectively.

• Journal of Life Science
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• v.13 no.6
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• pp.805-813
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• 2003

cDNA encoding somatolactin (SL) was obtained by RT-PCR from pituitary glands of rock bream (Oplegnathus fasciatus). The full length cDNA of rock bream somatolactin (rbSL) is 1636 bp long. It contains a 696 bp open reading frame encoding a signal peptide of 24 amino acids (an) and a mature protein of 207 aa. rbSL has seven cysteine residues$(Cys^{5},\; Cys^{15},\; Cys^{42},\; Cys^{65},\; Cys^{181},\; Cys^{198}\; $and $Cys^{206})$ and two potential N-glycosylation sites at positions $Asn^{121}$and $Asn^{153}$. The rbSL shares 61.1∼92.6% amino acid sequence similarities and 63∼92.6% nucleotide sequence identities with other teleost SLs, except for goldfish and channel catfish SL. Amino acid sequence alignment revealed that rbSL has four conserved domains $(A_{SL},\; B_{SL},\; C_{SL}and\; D_{SL})$ common to all SLs. Out of these domains, $(A_{SL},\; B_{SL},\; C_{SL}and\; D_{SL})$, are also conserved in all teleost growth hormones and prolactins. The cDNA of rbSL has been cloned into pET expression vector in order to produce recombinant rbSL in E. coli BL2l(DE3) cells. The recombinant protein showed a molecular weight of 27 kDa in SDS-PAGE.

• Journal of Life Science
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• v.26 no.6
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• pp.737-748
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• 2016

By this time, insect antimicrobial peptides (AMPs) have been characterized more than 150 peptides since purification of cecropin in the hemolymph of pupae from Hyalophora cecropia in 1980. Therefore, it is considered that insects are good sources of AMP selection. Insect AMPs are small (low molecular weight) and cationic, and amphipathic with variable length, sequence, and structure. They perform a pivotal role on humoral immunity in the insect innate immune system against invading pathogens such as bacteria, fungi, parasites, and viruses. Most of the insect AMPs are induced rapidly in the fat bodies and other specific tissues of insects after septic injury or immune challenge. Then the AMPs subsequently released into the hemolymph to act against microorganisms. These peptides have a broad antimicrobial spectrum against various microbes including anticancer activities. Insect AMPs could be divided into four families based on their structures and sequences. That is the α-helical peptides, cysteine-rich peptides, proline-rich peptides, and glycine-rich peptides/proteins. For instance, cecropins, insect defensins, proline-rich peptides, and attacins are common insect AMPs, but gloverins and moricins have been identified only in lepidopteran species. This review focuses on AMPs from insects and discusses current knowledge and recent progress with potential applications of insect AMPs.

• Journal of Life Science
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• v.17 no.10
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• pp.1341-1346
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• 2007

An intracellular ${\beta}-xylosidase$ from Paenibacillus sp. DG-22 was purified to homogeneity by ion-exchange, hydrophobic interaction and gel-filtration chromatography. The molecular weight of the enzyme was measured to be 156,000 by gel filtration and 80,000 by SDS-PAGE, indicating that the enzyme consisted of two identical subunits. The purified enzyme exhibited maximum activity at $65^{\circ}C$ and pH 5.5. It retained 89% of its initial activity up to 60 min at $60^{\circ}C$ and had a half-life of 25 min at $65^{\circ}C$. The enzyme was highly specific for pNPX as the substrate. It showed little or no activity against other p-nitrophenyl glycosides and xylans. The $K_m\;and\;V_{max}$ for pNPX was 0.53 mM and 3.18 U/mg protein, respectively. The ${\beta}-xylosidase$ was strongly inhibited by $Ag^+,\;Fe^{2+},\;Hg^{2+}\;and\;Zn^{2+}$ and slightly activated by DTT. The hydrolysis product from xylobiose, xylotriose, and xylotetraose was xylose.

• Journal of Life Science
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• v.17 no.10
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• pp.1321-1329
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• 2007

Deer antler tissue contains the most rapidly growing bone in the animal kingdom. Thus, it is likely that growing antler tissue is a rich source of local paracrine bone-stimulating factors. Growth factors, at least the insulin-like growth factor (IGF), control the bone-remodelling process. In this study, we tried to isolate and purify IGF-I from fresh antler tissue by the routine isolation and purification of protein. The purification involved ammonium sulfate precipitation, DEAE-Sepharose CL-60 ion-exchange chromatography, CM-Sepharose CL-6B ion-exchange chromatography, and Sephadex G-50 chromatography. Purified fractions from each step were analyzed by high-performance liquid chromatography (HPLC), SDS polyacrylamide gel electrophoresis (SDS-PACE), Dot-blot, and Western-blot methods. Furthermore, the quantification of partially purified IGF-I was calculated by enzyme-linked immunosorbent assays (ELISA) using antibody to human recombinant IGF-1. SDS-PAGE analysis of the final fraction yielded two molecular bands and the signal band was at 12 kDa on the Western-blot film. This purified IGF-I fraction showed a peak at retention time of eight min. The quantity of IGF-I in 20 g deer antler tissue as starting weight was calculated using a standard curve to be 2910 ng/ml, and total IGF-I amount is 0.291 g. The results show that IGF-I, which can be found in deer antler, can be partially purified and quantified by classic protein isolation methods.