• BMB Reports
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• v.41 no.5
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• pp.394-399
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• 2008

Multiple sequence alignments of the Bombyx mori fibroin light chain gene (fib-L) from hybrids and from Chinese and Japanese strains demonstrated that 51.6% of the fib-L third intron is conserved. One of these conserved segments, 41 bp long, contains the sequence CGTTATTATACATATT, which is duplicated in the B. mori Nd-$s^D$ mutant. In the present work, electrophoretic mobility assays and computational analyses revealed a major peak of intrinsic bent DNA within the segment that undergoes breakage in the previously-described Nd-$s^D$ mutation. This result suggested that this intrinsically-curved region might mediate DNA cleavage and enhance recombination events in the third intron of the Bombyx mori fib-L gene.

• Journal of Microbiology and Biotechnology
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• v.20 no.3
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• pp.460-466
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• 2010

A mutant of green fluorescent protein ($GFPmut3^*$) from the jellyfish Aequorea victoria was cyclized in vitro and in vivo by the use of a naturally split intein from the dnaE gene of Synechocystis species PCC6803 (Ssp). Cyclization of $GFPmut3^*$ was confirmed by amino acid sequencing and resulted in an increased electrophoretic mobility compared with the linear $GFPmut3^*$. The circular $GFPmut3^*$ was $5^{\circ}C$ more thermostable than the linear form and significantly more resistant to proteolysis of exopeptidase. The circular $GFPmut3^*$ also displayed increased relative fluorescence intensity. In addition, chemical stability of $GFPmut3^*$ against GdnHCl revealed more stability of the circular form compared with the linear form.

• Journal of Physiology & Pathology in Korean Medicine
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• v.22 no.5
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• pp.1309-1314
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• 2008

This study was undertaken to elucidate the antioxidant activity of the ethanol (EEPB) and water (WEPB) extracts of Prunus persica branches. The extracts contained a high phenolic content and revealed a potent hydrogen donating activity in DPPH scavenging assay. Compared to $\alpha$-tocopherol, EEPB (p < 0.001) and WEPB (p < 0.05) significantly inhibited $FeCl_2$-ascorbic acid-induced lipid peroxidation, and also exhibited potent antiradical activities against hydroxyl radical, superoxide anion, nitric oxide and peroxynitrite. In copper- and AAPH-mediated human low-density lipoprotein (LDL) oxidation systems, the extracts demonstrated a strong antioxidant function by metal chelating, rather than direct scavenging, action. Furthermore, EEPB at 5 ${\mu}g/mL$ concentration showed 80.77% inhibition of the electrophoretic mobility of LDL, compared to 77.69% for ascorbic acid and 76.92% for BHT. These results suggest that PB branch extracts may protect against oxidative stress-induced diseases.

• Korean Journal of Acupuncture
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• v.25 no.1
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• pp.113-130
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• 2008

Objectives : Hyangsapyungwisan (HPS) has been used for treatment of cardiovascular diseases including of arthralgia, myalgia in traditional Korean medicine. However, the medical actions of HPS have not been clearly investigated. The aim of this study was to elucidate the antiradical and antioxidant activity of the extract for herb-acupuncture (HPS-HA) obtained from HPS. Methods & Results : HPS-HA exhibited a stronger inhibition rate (55.5%) on lipid peroxidation of rat liver homogenate induced by $FeCl_2$-ascorbic acid. In addition, HPS-HA markedly interfered with hydroxylradical generation through iron ions chelating action. While pro-oxidant effect of HPS-HA was nearly undetectable at concentrations of 0.5-10㎎/mL. Moerover, HPS-HA revealed a potent antiradical activities on 2,2-diphenyl-1-picryl-hydrazyl (DPPH) radicals, superoxide anions, nitric oxide and peroxynitrite. Furthermore, HPS-HA inhibited copper- and AAPH-mediated oxidation of human low-density lipoprotein (LDL), and also suppressed the relative electrophoretic mobility of LDL. HPS-HA showed strong protective activity against oxidative damage of HUVECs induced by SIN-1. Conclusions : These results suggest that HPS-HA may be effective in protecting against oxidative diseases.

• Korean Journal of Microbiology
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• v.16 no.1
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• pp.30-40
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• 1978

Detergent soluble fractions were obtained from T. ferrooxidans ATCC 13598 and the T. thiooxidans ATCC 8085 which were treated with 3% of Tween 20. The detergent soluble antigen(crude antigen) fractions of the T.ferrooxidans and the T.thiooxidans were subjected to hydroxyapatite. In the case of T.thiooxidans, further purification was carried out on the DEAE-cellulose column chromatography. The antigen fractions, such as the hydroxyapatite peak-1(Tf, HA-1) and peak-2 from T.ferrooxidans(Tf. HA-2) and hydroxyapatite peak-1(Tt, HA-1), DEAE-cellulose peak-1(Tt, DP-1) and peak-2(Tt, DP-2) from T. thiooxidans wre compared each other with the homologous and the heterologous and the heterologous antisera against to the Thiobacillus species. The hydroxyapatite peak-2 fraction from the T.ferrooxidans(Tf, HA-2) and DEAE-cellulose peak-2 fraction from the T.thiooxidans(Tt, DP-2) were represented the type-specific immuno-reactivities between the T.ferrooxidans and the T.thiooxidans on the several sets of double gel diffusioin analysis. The type-specific antigen fractions from both of the baceteria were mainly composed of protein with entierly different electrophoretic mobility on the SDS-polyacrylamide gel electrophoresis. However, the PAS positive banding patterns on the electrophorogram showed wide range of common antigenic properties in the T. ferrooxidans and the T.thiooxidans, respectively.

• The Journal of Korean Medicine
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• v.23 no.1
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• pp.50-60
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• 2002

Objectives: Sunghyangjunggisan (SHJS) is a commonly prescribed drug with a wide neuropharmacological spectrum. The water extracts of SHJS were found to be protective against neurotoxicity elicited by deprivation of serum and glucose. Methods: The morphological examination and Hoechst staining of nucleus also clearly showed that the extracts attenuated the cell shrinkage, membrane blebbing, representing typical neuronal apoptotic phenomena and nucleosome-sized fragmentation under the microscope in PC 12 rat pheochromocytoma cells. Results: Activation of protein kinase A (PKA) with dibutyl-cAMP and forskolin also protected during glucose deprivation, although it was not additive with the effect provided by phorbol ester. Interestingly, treatment with the protein kinase A inhibitor, KT5720, was not neuroprotective in the presence of SHJS. Electrophoretic mobility shift assays were used to characterize the neuroprotective binding of nuclear proteins to consensus sequences for AP-l, nuclear factor kappa B ($NF-{\kappa}B$) after glucose deprivation. When PC 12 cells are induced to undergo apoptosis by serum deprivation, AP-l and $NF-{\kappa}B$ DNA binding activity transiently increases to a slight degree. This stimulation is blocked by the water extracts of SHJS. The site of action of the drugs appeared to involve specific inhibition of AP-1 and nuclear factor kB binding activity. Conclusions: Taken together, these results suggested the possibility that the extracts of SHJS might provide a neurotrophic-like activity in PC 12 cells.

• Journal of Microbiology and Biotechnology
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• v.22 no.5
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• pp.614-621
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• 2012

Silver nanoparticles production by the green chemistry approach was investigated using an isolated marine actinomycetes strain. The isolated strain was identified as Streptomyces albidoflavus based on chemotaxonomic and ribotyping properties. The strain revealed production of silver nanoparticles both extracellular and intracellularly. Surface Plasmon Resonance analysis with the function of time revealed that particle synthesis by this strain is reaction time dependent. The produced particles were spherical shaped and monodispersive in nature and showed a single surface plasmon resonance peak at 410 nm. Size distribution histograms indicated production of 10-40-nm-size nanoparticles with a mean size of 14.5 nm. FT-IR spectra of nanopartilces showed N-H, C-H, and C-N stretching vibrations, denoting the presence of amino acid/peptide compounds on the surface of silver nanoparticles produced by S. albidoflavus. Synthesized nanoparticles revealed a mean negative zeta potential and electrophoretic mobility of -8.5 mV and -0.000066 $cm^2/Vs$, respectively. The nanoparticles produced were proteinaceous compounds as capping agents with -8.5 mV zeta potential and revealed antimicrobial activity against both Gram-negative and -positive bacterial strains. Owing to their small size, these particles have greater impact on industrial application spectra.

• Carbon letters
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• v.7 no.1
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• pp.1-8
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• 2006

The activated carbon "C" was obtained by carbonization followed by activation with steam at 40% of burn-off. Oxidized carbons C-N, C-P and C-H were obtained by oxidizing the activated carbon C with concentrated nitric acid, ammonium peroxysulfate and hydrogen peroxide, respectively. The textural properties of the carbons were determined from nitrogen adsorption at 77 K. The acidic surface functional groups were determined by pH titration, base neutralization capacity and electrophoretic mobility measurements. The cation exchange capacities of un-oxidized and oxidized carbons were determined by the removal of Cu(II) and Ni(II) from their aqueous solutions. The surface area and the total pore volume decreased but the pore radius increased by the treatment of activated carbon with oxidizing agents. These changes were more pronounced in case of oxidation with $HNO_3$. The surface pH of un-oxidized carbon was basic whereas those of the oxidized derivative were acidic. The removal of Cu(II) and Ni(II) was pH dependent and the maximum removal of the both ions was obtained at pH of 5-6. Cu(II) was more adsorbed, a phenomenon which was ascribed to its particular electronic configuration.

• Journal of the Korean Society of Food Science and Nutrition
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• v.24 no.3
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• pp.362-370
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• 1995

Human plasma low density lipoprotein(LDL) is the main carrier for cholesterol, and recent studies suggest the normal LDL can be readily oxidized by free radical and not interact with LDL receptor. Lipoprotein pariticles are consisted of lipid andprotein, and fatty acids of lipoproteins are prone to oxidation. LDL particles readily undergo oxidative modification by copper. From the results, oxidized LDL altered its biological properties. A marked increase in the electrophoretic mobility of LDl on agarose gel indicated that negative surface charge of the LDL particles was increased. Also, the results from the HPLC showed that oxidized LDL was degraded into several polypeptides nonenzymatically. Degradation tests which measured the amount of 5-IAF labelled oxidized LDL were carried out by monocyte and hepatocyte cell culture. Hepatocyte cell culture of modified LDL did not show consistent pattern. However, binding rate of modified LDL with HMDM(human monocyte derived macrophage) was enhanced with oxidation, but was retarded by addition of antioxidants(hyaluronic acid, vitamin A, vitamin E). Also comparisons of oxidized-LDL, acetyl-LDL and MDA-LDL showed significant differences in the chemical properteis and binding affinity to HMDM. Thus, modificaition of normal LDL altered its biological properties.

• BMB Reports
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• v.41 no.11
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• pp.771-777
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• 2008

Calmodulin (CaM) proteins, members of the EF-hand family of $Ca^{2+}$-binding proteins, represent important relays in plant calcium signals. Here, OsCam1-1 was isolated by PCR amplification from the rice genome. The gene contains an ORF of 450 base pairs with a single intron at the same position found in other plant Cam genes. A promoter region with a TATA box at position-26 was predicted and fused to a gus reporter gene, and this construct was used to produce transgenic rice by Agrobacterium-mediated transformation. GUS activity was observed in all organs examined and throughout tissues in cross-sections, but activity was strongest in the vascular bundles of leaves and the vascular cylinders of roots. To examine the properties of OsCaM1-1, the encoding cDNA was expressed in Escherichia coli. The electrophoretic mobility shift when incubated with $Ca^{2+}$ indicates that recombinant OsCaM1-1 is a functional $Ca^{2+}$-binding protein. In addition, OsCaM1-1 bound the CaMKII target peptide confirming its likely functionality as a calmodulin.