• The Korean Journal of Food And Nutrition
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• v.33 no.3
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• pp.309-316
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• 2020

In this study, we investigated the protective effects of Ulva lactuca methanol extracts against ultraviolet B (UVB)-induced DNA damage in HaCaT cells. First, the contents of general and antioxidative nutrient contents of Ulva lactuca were measured. The moisture, carbohydrate, crude protein, crude fat and ash were 14.01%, 44.80%, 23.19%, 3.10% and 14.90%, respectively. Magnesium that acts as DNA repair enzyme cofactor was the most abundant mineral followed by Ca, P and Fe. The total phenolic and anthocyanoside contents of Ulva lactuca were 2.69 mg/g and 0.13 mg/g, respectively. Cells treated with Ulva lactuca methanol extracts for 24 hours post UVB exposure increased cell viability in a concentration-dependent manner compared to the non-treated control. Also, Ulva lactuca methanol extracts decreased the levels of UVB-induced DNA damage such as cyclobutane pyrimidine dimer and DNA damage response (DDR) proteins such as p-p53 and p21. These results suggest that Ulva lactuca methanol extracts comprising physiological active substances such as Mg, polyphenols and anthocyanosides promote DNA repair by regulating genes related with DDR.

• Proceedings of the Korean Society of Applied Pharmacology
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• 1995.04a
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• pp.80-80
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• 1995

T4 Endonuclease V (Mw 16,000) acts as a repair enzyme for UV induced pyrimidine dimers in DNA. Many researchers have studied the biochemical characteristics of the enzyme. However the precise action mechanism of T4 endo V has not fully elucidated yet. In our laboratory NMR spectroscopy technique is being used for the structural study of T4 endo V. Because of its low temperature stability and high content of ${\alpha}$-helix, the conventional $^1$H NMR technique was inapplicable. Therefore we utilized stable isotope labeling technique and so far prepared about 10 amino acid specific labeled proteins. The HSQC spectra of amino acid specific labeled proteins will help us to interpret the triple resonance 3D, 4D data which are under processing, We also studied the behaviors of specific amino acid residues whose roles might be critical. When the enzyme labeled by $\^$15/N-Thr was mixed with the substrate oligonucleotide (semispecific -TT- sequence), one crosspeak in its HSQC spectrum was completely desappeared, which means that one of seven Thr residues is in the binding site of the enzyme with DNA, This result is well consistent with previous report that implicated the Thr 2 residue in the activity of the enzyme. Similar studies were carried on the behaviors of Arg and Tyr residues.

• The Korean Journal of Nuclear Medicine
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• v.30 no.4
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• pp.532-540
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• 1996

목적 : 종양세포의 증식을 평가하기 위해 radiofluorinated ethyluracil (FEU)과 deoxyadenosine analogue(FAD)를 합성하여 종양의 영상화를 시도하였다. 대상 및 방법 : 5-(2-Fluoroethyl)uracil ([$^{18}F$]FEU)은 2, 4-dimethoxy-5-(2-hydroxyethyl) pyrimidine을 $K^{18}F$와 처리한 후 HBr로 가수분해하여 얻었으며 Fluorodeoxyadenosine은 adenosine의 triacetylated analogue를 $K^{18}F$와 처리하여 얻었다. 생물학적 조직분포는 유방암 세포(13762 NF, 100,000 cells per rat, im)를 쥐에 접종한 후 0.5, 1, 2 및 4시간에 주요장기를 적출하여 %ID/g을 측정하고 자가방사영상은 방사성의약품 투여 45분 후에 얻었다. PET 영상은 VX-2 종양을 접종한 가토를 이용하여 얻었다. In vitro cell proliferation assay는 사람의 말초단핵구를 이용하였다. 결 과 : In vitro assay상 ([$^{18}F$]FEU는 세포증식시 DNA/RNA에 결합함을 시사하였다. ([$^{18}F$]FAD와 ([$^{18}F$]FEU의 종양/비종양 방사능 섭취비는 시간경과에 따라 증가하였으며 ([$^{18}F$]FAD와 ([$^{18}F$]FEU를 이용한 자가방사영상과 ([$^{18}F$]FEU를 이용한 PET 영상에서 종양을 잘 관찰할 수 있었다. 결 론 : ([$^{18}F$]FAD 및 ([$^{18}F$]FEU를 이용하여 종양세포의 증식을 PET 영상에서 평가할 수 있으리라 사료된다.

• Journal of Microbiology and Biotechnology
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• v.15 no.3
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• pp.484-490
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• 2005

Human ribosomal protein S3 (rpS3), which has a DNA repair endonuclease activity, is a multifunctional protein. This protein is involved in DNA repair, translation, and apoptosis. In particular, rpS3 has a lyase activity, which cleaves the phosphodiester bond of damaged sites such as cyclobutane pyrimidine dimers and AP sites. Here, using deletion analysis, we identified that the repair endonuclease domain resides in the C-terminal region (165-243 aa) of rpS3. We also found that ectopic expression of GST-rpS3 in bacterial strain BL21 promoted the resistance of these cells to ultraviolet (UV) radiation and hydrogen peroxide ($H_{2}O_{2}$) treatment. The repair domain of rpS3 was sufficient to exhibit the resistance to UV irradiation and recover cell growth and viability, showing that the repair activity of rpS3 is responsible for the resistance to UV irradiation. Our study suggests that rpS3 is able to process DNA damage in bacteria via its repair domain, showing the resistance to genotoxic stress. This implies that rpS3-like activity could be operative in bacteria.

• Animal cells and systems
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• v.2 no.3
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• pp.355-359
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• 1998

Among the proteins secreted from Lactobacillus acidophilus KCTC 3151, a 36 kDA and 24 kDa protein, whose amounts were relatively abundant, were purified and their N-terminal amino acid sequences determined. The N-terminal amino acid sequence of 36 kDa protein exhibited high homology with thymidine phosphorylase and glyceraldehyde-3-phosphate dehydrogenase. The N-terminal amino acid sequence of the 24 kDa protein did not show significant homology with proteins in Protein Data Base nor Gene Bank. Nucleotide sequence of the gene encoding 36 kDa protein indicates that the protein possesses the domains for a-helical, phosphate binding and pyrimidine binding sites, which are also shown in thymidine phosphorylases. Also, the protein contains conserved domains of dehydrogenase II and III. However, the activity of thymidine phosphorylase or glyceraldehyde-3-puospnate dehydrogenase could not be detected in the purified fractions of the 36 kDa protein.

• Microbiology and Biotechnology Letters
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• v.21 no.1
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• pp.23-29
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• 1993

A bacterial strain. producing a nucleoside oxidase was isolated from soil and identified as Flavobacterium meningosepticum by its taxonomical characteristics. The enzyme has been purified ISO-fold to electrophoretic homogeniety in an overall yield of 18% from the cell free extract of the producer. The enzyme catalyzed oxidation of only nucleosides related to both purine and pyrimidine with very high substrate specificity. The nucleoside oxidase was proved to be a noble enzyme by stoichiometry that 1 mol adenosine as a substrate was especially oxidized via adenosine 5' -aldehyde to 1 mol adenosine 5' -carboxylic acid with the formation of 2 mol $H_20_2$

• Journal of the Korean Chemical Society
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• v.56 no.3
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• pp.334-340
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• 2012

A new series of ethyl 2-(4-substitutedbenzylidene)-5-(3'-(ethoxycarbonyl)biphenyl-4-yl)-7-methyl-3-oxo-3,5-dihydro-2H-thiazolo[3,2-a]pyrimidine-6-carboxylate derivatives ($\mathbf{8a-j}$) were synthesized. The newly synthesized compounds were characterized by $\mathbf{IR}$, $^1\mathbf{H}$ $\mathbf{NMR}$, $^{13}\mathbf{C}$ $\mathbf{NMR}$, $\mathbf{LCMS}$ $\mathbf{mass}$ and $\mathbf{C}$, $\mathbf{H}$, $\mathbf{N}$ analyses. All newly synthesized compounds were screened for their In vitro antioxidant activity (Scavenging of hydrogen peroxide, Scavenging of nitric oxide radical, and Lipid peroxidation inhibitory activity), antibacterial (Escheria coli, Pseudonmonas aeruginosa (gram-negative bacteria), Bacillus subtillis, Staphylococcus aureus (gram-positive bacteria)) and antifungal (Candida albicans Aspergillus niger) studies.

• Bulletin of the Korean Chemical Society
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• v.33 no.12
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• pp.4074-4078
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• 2012

The first step in the common pathway for the biosynthesis of branched chain amino acids is catalyzed by acetohydroxyacid synthase (AHAS). The AHAS is found in plants, fungi and bacteria. With an aim to identify new anti-tuberculosis drugs that inhibit branched chain amino acid biosynthesis, we screened a chemical library against Mycobacterium tuberculosis AHAS. The screening identified four compounds, AVS 2087, AVS 2093, AVS 2236, and AVS 2387 with $IC_{50}$ values of 0.28, 0.21, 3.88, and $0.25{\mu}M$, respectively. Moreover, these four compounds also showed strong inhibition against reconstituted AHAS with $IC_{50}$ values of 0.37, 0.26, 1.0, and $1.18{\mu}M$, respectively. The basic scaffold of the AVS group consists of 1-pyrimidin-2-yl-1H-[1,2,4]-triazole-3-sulfonamide. The most active compound, AVS 2387, showed the lowest total interaction energy -8.75 Kcal/mol and illustrates its binding mode by hydrogen bonding with $H_{\varepsilon}$ of Gln517 with the distance of $2.24{\AA}$.

• Bulletin of the Korean Chemical Society
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• v.34 no.8
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• pp.2291-2296
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• 2013

An efficient carbon monoxide (CO) sensor was developed based on poly(3,4-ethylenedioxy)thiophenepoly(styrenesulfonate) (PEDOT:PSS) modified with a new pyrimidine-fused heterocyclic compound, bis(2-hydroxyphenyl)dihydropyrido[2,3-d:6,5-d]dipyrimidine-tetraone (B2HDDT). B2HDDT remains stable in the polymer matrix through interactions with functional groups of the polymer. It created prominent sites that captured CO gas, and the experimental parameters, including the amount of doped B2HDDT in the PEDOT:PSS film, were optimized. The sensor probe was also examined to verify its reliability for detecting CO in the presence of atmospheric gases in a discriminating manner. NMR, AFM, and FT-IR spectra were obtained to evaluate the structure and morphology of the B2HDDT-doped PEDOT:PSS (PEDOT:PSS/B2HDDT) film. The content of 35 vol % B2HDDT (7.0 mM) in PEDOT:PSS provided the largest response factor (${\Delta}R/R_o$) for the CO gas. The sensor response was reproducible, with a relative standard deviation < 5% (n = 5). The detection limit was determined to be $0.44{\pm}0.05$ vol %.

• YAKHAK HOEJI
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• v.43 no.6
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• pp.756-761
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• 1999

Lipid peroxidation mediated by hydroxyl radicals which are generated during myocardial ischermia has suggested as a possible mechanism of ischemic myocardial damage. Recently, it has been reported that anti-arrhythmic action of lidocaine, a local anesthetic, is attributed to its "membrane-stabilizing" properties through scavenging free radicals, thus, inhibiting lipid peroxidation. Aldehyde oxidase and xanthine oxidase which catalyze the oxidation of many purine, pyrimidine and pteridine derivatives are known as free radical generating systems. In this experiment, we studied the effect of lidocaine and procainamide on the hepatic aldehyde and xanthine oxidase activity and antioxidative activities. It was found that lidocaine and procainamide inhibited both NADPH-dependent and independent lipid peroxidation. Both of tested compounds were found to be ineffective in inhibiting xanthine oxidase. Lidocaine and procainamide, however, inhibited aldehyde oxidase activity in vitro as well as in vivo. Based on the above results, lidocaine and procainamide could be employed as a therapeutic agent for aldehyde oxidaserelated disease.d disease.