• Journal of Microbiology
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• v.33 no.4
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• pp.283-288
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• 1995

We have identified hemolysin rendering virulency of Vibrio anguilarum grown at 23.deg.C which was evaluated on human RBCs. Hemolysin itself was separated as a single band on non-denaturing gel electrophoresis. Vibrio hemolysin was destroyed by trypsin and proteinase K and was heat labile. Optimal pH for activity was around pH 6 while pI of the molecule was recognized as 5.7, with relative distance (R$\sub$f/) on non-denaturing gel was 0.7. Addition of EDTA and FeCI$\sub$3/ drew the possibility that the production of hemolysin was mainly induced to overcome iron deficiency inside host animalsd infection.

• The Korean Journal of Zoology
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• v.38 no.4
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• pp.557-564
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• 1995

The 90 kDa-heat shock protein (HSP90) is one of the major ubiquitous heat shock proteins induced by a vadety of ceilular stresses. HSP90 Is constitutively synthesized even under nonstressed condidons and found In association with several regulatory and structural proteins such as protein kinases and steroid hormone receptors. In the present study, to facilitate its biochemical characterization, HSP90 was pudfied from chick muscle by sequential column chromatography steps including DEAE- cellulose, hydroxyapatite, and Sephacryl S-300 gel filtration and monoclonal antillodies specific to HSP90 were produced by the inurine hybridomal technique. We report the production of 4 posItive hybridoma clones, named as A204, C112, C302 and A204, C112, C302. Among these MoAbs, Cl 12 strongly reconnized chick HSP90 in Western blot and native immunoprocipitation. In addition, C112 showed the crossreactivitles against HSP90 from human, rabbit, mouse, fish and chick but not from Drosophila and E. coil.

• Analytical Science and Technology
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• v.27 no.6
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• pp.314-320
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• 2014

$La_{2-x}(MoO_4)_3:Er^{3+}/Yb^{3+}$ particles with doping concentrations of $Er^{3+}$ and $Yb^{3+}$ ($x=Er^{3+}+Yb^{3+}$, $Er^{3+}$=0.05, 0.1, 0.2 and $Yb^{3+}$ = 0.2, 0.45) were successfully prepared by the microwave-modified sol-gel method, and the upconversion photoluminescence properties were investigated. Well-crystallized particles, formed after heat-treatment at $900^{\circ}C$ for 16 h, showed a fine and homogeneous morphology with particle sizes of $2-5{\mu}m$. Under excitation at 980 nm, $La_{1.7}(MoO_4)_3:Er_{0.1}Yb_{0.2}$ and $La_{1.5}(MoO_4)_3:Er_{0.05}Yb_{0.45}$ particles exhibited a strong 525 nm emission band, a weak 550 nm emission band in the green region, and a very weak 655 nm emission band in the red region. The Raman spectra of the doped particles indicated the presence of strong peaks at higher frequencies of 752, 846, 922, 1358 and $1435cm^{-1}$ and lower frequency of $314cm^{-1}$ induced by the disorder of the $[MoO_4]^{2-}$ groups with the incorporation of the $Er^{3+}$ and $Yb^{3+}$ elements into the crystal lattice or by a new phase formation.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.35 no.4
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• pp.309-314
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• 2002

Rhtological properties of surimi gel from white fishes by acid (acid surimi) and alkali (alkali surmi) process and effect of chemicals on gelation were investigated by punch and dynamic tests. The breaking force and deformation values of heat-induced gel of acid surimi were less than their values of alkali and conventional surimi gel, and whiteness was greatly decreased, Gel point of acid surimi was decreased but it of alkali surimi was increased with increasing moisture content in the range of 80 to $85\%$. Storage modulus of acid surimi was the highest vaule in pH 6.8, but that of alkali surimi showed high value at neutral and slightly alkali pH. Propylene glycol increased storage modulus in $20\~50^{\circ}C$, hut urea and 2-mercaptoethanol suppressed it. Potassium bromide improved storage modulus in $20~80^{\circ}C$, The results suggest that alkai process is used for making surimi instead of conventional method.

• Journal of the Korean Society of Food Science and Nutrition
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• v.31 no.3
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• pp.438-444
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• 2002

Interactions between meat proteins and hydrocolloids in a model system may play an important role for the improvement of textural properties in low-fat sausage mixtures. The objective of this study was to determine gel properties as affected by the type and level of hydrocolloid, various pH values of meat protein-hydrocolloid mixture before cooking, and internal cooking temperatures. The desirable heat-induced gels (HIGs) were formed at least pH values above 6.0. The addition of konjac flour (KF), kappa-carrageenan (CN) and locust bean gum (LBG) to extracted salt soluble proteins (2%) improved the gel strength with increased levels (0.5∼1.5%) and HIGs containing CN had the highest (p<0.05) gel strength. The increase of cooking temperature increased gel strength, depending on pH and type of hydrocolloid. However, the minimun internal cooking temperature to make viscoelastic HIGs was 70$^{\circ}C$. These results indicated that desirable HIGs were manufactured with each hydrocolloid concentration of 1% and minimum cooking temperature of 70$^{\circ}C$ with pH values higher than 6.0.

• Animal cells and systems
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• v.1 no.3
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• pp.457-462
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• 1997

Antibacterial activity was induced in the haemolymph of the common cutworm, Spodoptera litura by the artificial injection of E, coli Ek132. Antibacterial peptides were purified from the immunized haemolymph by heat treatment, ion-exchange chromatography, gel filtration chromatography, and reverse phase FPLC, and their physicochemical characteristics were investigated. These purified antibacterial peptides designated as spodopsin la and Ib were named after Spodoptera litura. Spodopsin la and Ib had the apparent molecular masses of 3, 823 Da and 3, 886 Da, respectively, and about 20% of the sequences had basic amino acids, such as lysine and arginine but no cysteine. Also, spodopsin l was confirmed to be a new member of cecropin family having a similar amino acid sequence to cecropin of lepidopteran insects, such as Bombyx mori and Hyalophora cecropia. The purified spodopsin was active against gram-positive as well as gram-negative bacteria.

• Molecules and Cells
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• v.19 no.3
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• pp.328-333
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• 2005

Small heat shock proteins (sHSPs) are widely distributed, and their function and diversity of structure have been much studied in the field of molecular chaperones. In plants, which frequently have to cope with hostile environments, sHSPs are much more abundant and diverse than in other forms of life. In response to high temperature stress, sHSPs of more than twenty kinds can make up more than 1% of soluble plant proteins. We isolated a genomic clone, NtHSP18.3, from Nicotiana tabacum that encodes the complete open reading frame of a cytosolic class I small heat shock protein. To investigate the function of NtHSP18.3 in vitro, it was overproduced in Escherichia coli and purified. The purified NtHSP18.3 had typical molecular chaperone activity as it protected citrate synthase and luciferase from high temperature-induced aggregation. When E. coli celluar proteins were incubated with NtHSP18.3, a large proportion of the proteins remained soluble at temperatures as high as $70^{\circ}C$. Native gel analysis suggested that NtHSP18.3 is a dodecameric oligomer as the form present and showing molecular chaperone activity at the condition tested. Binding of bis-ANS to the oligomers of NtHSP18.3 indicated that exposure of their hydrophobic surfaces increased as the temperature was raised. Taken together, our data suggested that NtHSP18.3 is a molecular chaperone that functions as a dodecameric complex and possibly in a temperature-induced manner.

• Korean Journal of Microbiology
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• v.38 no.2
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• pp.67-73
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• 2002

The cellular responses of soil-borne bacterium, Pseudomonas sp. HK-6 to explosive 2,4,6-trinitrotoluene (TNT) were examined. Two stress shock proteins (SSPs), approximately 70-kDa DnaK and a 60-kDa GroEL were found in HK-6 cells in response to TNT. Analyses of SDS-PAGE and Western blot using anti-DnaK and GroEL revealed that SSPs were induced in HK-6 cells exposed to 0.5 M of TNT far 6-12 hrs. The maximum induction of proteins was achieved at 8-hr incubation point after HK-6 cells'exposure to TNT. Similar SSPs were found to be induced in HK-6 cells by heat shock (shift of temperature, from $30^{\circ}C$ to $42^{\circ}C$) or cold shock (shift of temperature,$30^{\circ}C$ to $4^{\circ}C$).2D-PAGE of soluble protein tractions from the culture of Pseudomonas sp. HX-6 exposed to TNT demonstrated that approximately 450 spots were observed on the silver stained gels ranging from pH 3 to pH 10. Among them, 12 spots significantly induced and expressed in response to TNT were selected and analyzed. Approximately 60-kDa protein, which was assumed highly expressed on the gel, was used for amino acid sequencing. N-terminal microsequencing with in-gel digestion showed that N-terminal sequence of the TNT-induced protein, <$^1XXAKDVKFGDSARKKML^17$, shared extensive similarity with $^1XXAKDVKFGDSARKKML^17$, N-terminal sequence of (P48216) GroEL of Pseudomonas putida.

• Asian-Australasian Journal of Animal Sciences
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• v.32 no.5
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• pp.721-733
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• 2019

Objective: The objectives of this study were to investigate the thermal gelation properties and molecular forces of actomyosin extracted from two classes of chicken breast meat qualities (normal and pale, soft and exudative [PSE]-like) during heating process to further improve the understanding of the variations of functional properties between normal and PSE-like chicken breast meat. Methods: Actomyosin was extracted from normal and PSE-like chicken breast meat and the gel strength, water-holding capacity (WHC), protein loss, particle size and distribution, dynamic rheology and protein thermal stability were determined, then turbidity, active sulfhydryl group contents, hydrophobicity and molecular forces during thermal-induced gelling formation were comparatively studied. Results: Sodium dodecyl sulphate-polyacrylamide gel electrophoresis showed that protein profiles of actomyosin extracted from normal and PSE-like meat were not significantly different (p>0.05). Compared with normal actomyosin, PSE-like actomyosin had lower gel strength, WHC, particle size, less protein content involved in thermal gelation forming (p<0.05), and reduced onset temperature ($T_o$), thermal transition temperature ($T_d$), storage modulus (G') and loss modulus (G"). The turbidity, reactive sulfhydryl group of PSE-like actomyosin were higher when heated from $40^{\circ}C$ to $60^{\circ}C$. Further heating to $80^{\circ}C$ had lower transition from reactive sulfhydryl group into a disulfide bond and surface hydrophobicity. Molecular forces showed that hydrophobic interaction was the main force for heat-induced gel formation while both ionic and hydrogen bonds were different significantly between normal and PSE-like actomyosin (p<0.05). Conclusion: These changes in chemical groups and inter-molecular bonds affected protein-protein interaction and protein-water interaction and contributed to the inferior thermal gelation properties of PSE-like meat.

• Korean Journal of Materials Research
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• v.25 no.9
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• pp.480-486
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• 2015

$Pb_{1-x}MoO_4:Er^{3+}/Yb^{3+}$ phosphors with various doping concentrations of $Er^{3+}$ and $Yb^{3+}$ ($x=Er^{3+}+Yb^{3+}$, $Er^{3+}=0.05$, 0.1, 0.2, and $Yb^{3+}=0.2$, 0.45) are successfully synthesized using a microwave sol-gel method, and the up-conversion photoluminescence properties are investigated. Well-crystallized particles, which are formed after heat treatment at $900^{\circ}C$ for 16 h, exhibit a fine and homogeneous morphology with particle sizes of $2-5{\mu}m$. Under excitation at 980 nm, the $Pb_{0.7}MoO_4:Er_{0.1}Yb_{0.2}$ and $Pb_{0.5}MoO_4:Er_{0.05}Yb_{0.45}$ particles exhibit a strong 525 nm emission band, a weak 550 nm emission band in the green region, and a very weak 655 nm emission band in the red region. The Raman spectra of the doped particles indicate the presence of strong peaks at higher and lower frequencies induced by the disordered structures of $Pb_{1-x}MoO_4$ through the incorporation of the $Er^{3+}$ and $Yb^{3+}$ ions into the crystal lattice, which results in the unit cell shrinkage accompanying the new phase formation of the $MoO_{4-x}$ group.