• Journal of radiological science and technology
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• v.38 no.3
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• pp.253-259
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• 2015

The information of contrast media concentration on target organ is very important to get reduce the side effect and high contrast imaging. We investigated alternation of signal intensity as a function of the modality of Gd-based contrast media on spin echo and ultra short time echo (UTE) of T1 effective pulse sequence at 3T MRI unit. Gadoxetic acid, which is a MRI T1 contrast medium, was used to manufacture an agarose phantom diluted in various molarities, and sterile water and agarose 2% were used as the buffer solution for the dilution. The gold standard T1 calculation was based on coronal single section imaging of the phantom mid-point with 2D Inversion recovery spine-echo pulse sequence MR imaging for testing of phantom accuracy. The 1-2mmol/L and 7mmol/L was shown the maximum signal intensity on spin echo and UTE respectively. We confirm the difference of contrast media concentration which was shown the maximum signal intensity depending on the T1 effective pulse sequence.

• KSBB Journal
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• v.14 no.1
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• pp.96-102
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• 1999

Marine bacterium Bacillus cereus ASK202 produced an extracellular agarase (E.C.3.2.1.81) which showed a high level of enzyme activity in the presence of agar and agarose. In the optimal culture conditions, the agarase production increased 7.7 folds compared with the one obtained from the basal medium. Agarase production reached upto 160 units/L after 24hr of cultivation in a modified marine medium at $25^{\circ}C$. The degree of purification increased 31.5 folds with 27.8% yield through freeze drying, DEAE Sepharose CL-6B and Superose 6HR 10/30 column chromatography. The molecular weight of the purified agarase was determined to be 90,000 daltons by gel-permeation filteration. Optimal temperature and pH for the enzyme activity were $40^{\circ}C$ and 7.8, respectively. The enzyme was stable up to $50^{\circ}C$ and at a broad pH range of 5.0-10.0. The $\beta$-agarase was activated by $Zn(NO_3)_2$, and was inhibited by $CuSO_4$ and $SnCl_2$. The Km and Vmax values of this enzyme for agarose as a substrate was $2.4mg/m\ell$ and 13.6 mg/m$\ell$, respectively.

• Journal of Applied Biological Chemistry
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• v.52 no.4
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• pp.157-162
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• 2009

An agar-liquefying bacteria (SC-22), which produces a diffusible agarase that caused agar softening around the colony was isolated from Daecheong lake in Korea. Chemotaxanomic and phylogenetic analyses based on 16S rRNA gene sequences revealed the strain was classified as Cellvibrio mixtus SC-22. The isolate SC-22 showed maximal extracellular agarase activity with 58.5 U/mL after 48 h cultivation in the presence of 0.2% agar. It was observed that the isolate produced two kinds of extracellular and three kinds of intracellular isoenzymes. The major agarase was purified from the culture filtrate of agarolytic bacteria by ammonium sulfate precipitation, anion exchange and gel filtration column chromatographic methods. The molecular mass of the purified enzyme was estimated to be 25 kDa by SDS-PAGE. The optimum pH and temperature of the purified enzyme were pH 7.0 and $50^{\circ}C$, respectively. The agarase activity was activated by $Fe^{2+}$, $Na^+$ and $Ca^{2+}$ ions while it was inhibited by $Hg^{2+}$, $Mn^{2+}$ and $Cu^{2+}$ at 1 mM concentration. The predominant hydrolysis product of agarose by the enzyme was galactose and disaccharide on TLC, indicating the cleavage of $\beta$-1,4 linkage in a random manner. The enzyme showed high substrate specificity for only agar and agarose among various polysaccharides.

• Journal of Life Science
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• v.22 no.5
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• pp.627-633
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• 2012

$Microbulbifer$ sp. AJ-3 was used to acquire the degrading products from $Capsosiphon$ $fulvescens$ (DPCF), which were investigated to determine its physiological activities. A crude enzyme extract from $Microbulbifer$ sp. AJ-3 hydrolyzes polysaccharide substrates such as agar, agarose, alginic acid, fucoidan, laminaran, starch, and chitin. Among them, agarose, laminaran, and alginic acid showed higher activities, especially alginic acid. The antioxidant activity of DPCF was measured by using 2,2-diphenyl-1-picryl-hydrazyl (DPPH) and superoxide dismutase (SOD)-like activities and were about 32% and 93% at 2 mg/ml, respectively. In addition, the nitrite-scavenging activity of DPCF was about 82%, 53%, and 12% at pH levels of 1.2, 3.0, and 6.0, respectively. To determine the influence of DPCF on alcohol metabolism, the generating activity of reduced-nicotinamide adenine dinucleotide (NADH) by alcohol dehydrogenase (ADH) was measured. The facilitating rate of ADH activity by DPCF was 130% at 2 mg/ml. The tyrosinase inhibitory activity of DPCF was slightly increased in a dose-dependent manner and was about 28% at 2 mg/ml. These results indicated that the enzymatic products from DPCF have a strong antioxidant, nitrite scavenging, and alcohol metabolizing activity.

• Korean Journal of Microbiology
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• v.51 no.2
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• pp.115-125
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• 2015

A monoclonal antibody AP64 IgM binds to human acute nonlymphocytic leukemia (ANLL) cell line HL60 and also cross-reacts with the homologous antigen in a rat ANLL cell. This antibody mediated by complement, has leukemia a suppression effect. In this study, we generated a recombinant single-chain variable domain fragment (ScFv) which were derived from $V_H$ and $V_L$ cDNA of AP64 IgM-secreting hybridoma by RT-PCR. The two variable regions were joined with a single 15 amino acid linker $(G_4S)_3$. This recombinant ScFv was expressed as a single polypeptide chain from Escherichia coli BMH 71-18. The recombinant ScFv was purified by applying the periplasmic extract to $Ni^+$-NTA-agarose affinity column and detected with westernblot. The purified recombinant ScFv recognized a surface antigen (about 30 kDa) of HL60 cell line which is the same antigen detected by parental AP64 IgM. But the affinity of ScFv for a surface antigen of HL60 was lower than that of the parental AP64 IgM, which needs to be further improved. Overall, the recombinant ScFv specific to HL60 might be a useful bioreagent for either diagnostic or therapeutic purposes.

• Journal of Life Science
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• v.29 no.2
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• pp.158-163
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• 2019

The purpose of this study was to isolate a new marine agarase-producing bacterium. Agarase can hydrolyze agar and agarose to produce agarooligosaccharides or neoagarooligosaccharides, which possess many physiological functions. Strain DH-3 was isolated from seawater collected from the coast of Yeosu at Jeollanam province, Korea. A 16S rDNA sequence analysis showed this strain to be Persicobacter sp. DH-3. Extracellular agarase was prepared from culture media of Persicobacter sp. DH-3 and used for characterization. Relative activities at 20, 30, 40, 50, 60, and $70^{\circ}C$ were 50, 55, 70, 100, 90, and 50%, respectively. Relative activities at pH 5, 6, 7, and 8 were 75, 100, 90, and 75%, respectively. The enzyme showed maximum activity at $50^{\circ}C$ in a 20 mM Tris-HCl buffer at pH 6. This enzyme could be useful, as agar is in liquid state at $50^{\circ}C$. Agarase activities were maintained at 80% or more for 2 hr at 20, 30, and $40^{\circ}C$. Thin layer chromatography analysis suggested that Persicobacter sp. DH-3 produced extracellular ${\beta}$-agarases as it hydrolyzed agarose to produce neoagarohexaose and neoagarotetraose. In addition, zymogram analysis confirmed that Persicobacter sp. DH-3 produces at least three agar-degrading enzymes with molecular weights of 45, 70, and 140 kDa. Therefore, it is expected that agarases from Persicobacter sp. DH-3 could be used to produce functional neoagarooligosaccharides.

• Journal of Microbiology and Biotechnology
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• v.8 no.2
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• pp.182-184
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• 1998

PCR was used for quantitative counting of Bifidobacterium spp. in a sample mixed with Lactobacillus acidophilus using two primer sets; one set for universal priming and the other set for Bifidobacterium specific priming. DNA products from two independent PCRs with DNA extracted from the mixed sample were found to be easily distinguishable from each other by agarose gel electrophoresis. The concentrations of PCR products correlated with the total number of bacteria and with the number of Bifidobacterium spp. present in the sample.

• Microbiology and Biotechnology Letters
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• v.44 no.1
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• pp.106-106
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• 2016

• Archives of Pharmacal Research
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• v.24 no.5
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• pp.431-436
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• 2001

The water extract of Cichorium intybus (WECI) showed a remarkable antioxidative effect on LDL, and inhibitory effects on the production of thiobarbituric acid reactive substance and the Degradation of fatty acids in LDL. Vitamin 1 and unsaturated fatty acids in LDL were protected by adding WECI from the effects of metal catalyzed LDL oxidation. From the results obtained, we conclude that LDL oxidation is inhibited in vitro by the addition of WECI, and that LDL is protected by WECI from oxidative attack, as shown by agarose gel electrohporesis.

• Proceedings of the PSK Conference
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• 2003.10b
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• pp.159.2-159.2
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• 2003

Codonopside lc is an active natural compound isolated from the roots of Codonopsis lanceolata (Campanulaceae), a Korean medicinal herb. In the present study, we investigated the in vitro effect of Codonopside 1c on the proliferation and induction of apoptosis in HL-60 human promyelocytic cells. When HL-60 cells were treated with Codonopside 1c, evidence of apoptotic features, including DNA fragmentation, formation of DNA ladder in agarose gel elecrophoresis and increse of annexin V binding, were obtained. (omitted)