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Use of Li-K-Cd Alloy to Remove MCl3 in LiCl-KCl Eutectic Salt
Gha-Young Kim,Tack-Jin Kim,Junhyuk Jang,Si-Hyung Kim,Chang Hwa Lee,Sung-Jai Lee 한국방사성폐기물학회 2018 방사성폐기물학회지 Vol.16 No.3
Li-Cd 합금을 이용한 환원추출방식을 LiCl-KCl 기반의 drawdown 공정에 적용하게 되면, LiCl-KCl 공융염의 조성이 파괴되므로 공정온도를 높여야 하며, 전해정련 및 전해제련과 같은 공정에 LiCl-KCl 용융염을 재사용할 수 없게 된다. 따라서, 본 연구에서는 공융염 조성에 적합한 Li-K-Cd 합금을 제조하였으며, 이를 이용하여 U와 Nd가 포함된 LiCl-KCl 염에 투입하여 용 융염 내 UCl3의 제거가 가능한지 평가하였다. In this study, we prepared Li-K-Cd alloy, which meets the requirement of eutectic ratio of Li:K, to maintain the operating temperature of the drawdown process at 500℃ and to achieve the reuse of LiCl-KCl molten salt. The prepared Li-K-Cd alloys were added to LiCl-KCl salt bearing U and Nd at 500℃ to investigate the removal of UCl3 in the salt. The reduction of UCl3 in the salt was examined by measuring the OCP value of salt and analyzing the salt composition by ICP-OES. Reduction was also visually confirmed by change of salt color from dark purple to white. The experimental results reveal that the prepared Li-K-Cd alloy has reductive extractability for UCl3 in salt. By improving the preparation method, the Li-K-Cd alloy can be applied to the drawdown process.
Quantitative Detection of E. coli O157:H7 eaeA Gene Using Quantum Dots and Magnetic Particles
Kim, Gha-Young,Son, Ah-Jeong 한국생물공학회 2010 Biotechnology and Bioprocess Engineering Vol.15 No.6
A quantitative gene detection technique targeting the pathogenic E. coli O157:H7 eaeA gene was developed using magnetic bead (MB)-quantum dots (QDs) nanoparticle complexes. MBs allowed for the separation of DNA-conjugated QD nanoparticles via magnetic field manipulation. QDs provided internal fluorescence calibration to account for the intrinsically different numbers of nanoparticles interrogated in each assay. Based on the measurement of normalized fluorescence (Cy3/$QD_{655}$), the linear quantification ranges of ssDNA and dsDNA targets were determined to be 10 through $10^3$ fM ($R^2$ = 0.992) and $2{\times}10^2$ through $6{\times}10^7$ gene copies ($R^2$ = 0.972), with detection limits of 9.72 fM and 104 gene copies, respectively. The kinetic results indicate that adjustment of hybridization temperature in accordance to the amount of target DNA was required to maximize the efficiency of DNA hybridization. We were able to discriminate perfectly matched target DNA, 1-, 2-, and 41-base pair mismatched target DNAs in our approach and therefore demonstrated excellent selectivity. Our technique was also used on pure bacterial culture to showcase its ability to analyze environmental samples.
PIASy-Mediated Sumoylation of SREBP1c Regulates Hepatic Lipid Metabolism upon Fasting Signaling
Lee, Gha Young,Jang, Hagoon,Lee, Jae Ho,Huh, Jin Young,Choi, Sekyu,Chung, Jongkyeong,Kim, Jae Bum American Society for Microbiology 2014 Molecular and cellular biology Vol.34 No.6
<P>SREBP1c is a key transcription factor that regulates <I>de novo</I> lipogenesis during anabolic periods. However, the molecular mechanisms involved in the suppression of SREBP1c under nutritional deprivation are largely unknown. In this study, we demonstrate that the small ubiquitin-related modifier (SUMO) E3 ligase, a protein inhibitor of activated STAT Y (PIASy), sumoylates SREBP1c at Lys98, leading to suppression of the hepatic lipogenic program upon fasting-induced signals. In primary hepatocytes, ablation of PIASy stimulated intracellular lipid accumulation through the induction of SREBP1c and its target genes. Given that protein kinase A (PKA) plays important roles in catabolic responses, activated PKA enhances the sumoylation of SREBP1c and potentiates the interaction between SREBP1c and PIASy. Notably, overexpression of PIASy in obese <I>db/db</I> mice ameliorated hepatic steatosis, while suppression of PIASy in lean (wild-type) mice stimulated hepatic lipogenesis with increased expression of SREBP1c target genes. Furthermore, PKA-mediated SREBP1c phosphorylation augmented SREBP1c sumoylation, subsequently leading to degradation of SREBP1c via ubiquitination. Together, these data suggest that PKA-induced SREBP1c sumoylation by PIASy is a key regulatory mechanism to turn off hepatic lipogenesis during nutritional deprivation.</P>
Kim, Gha-Young,Shim, Joonmok,Kang, Min-Su,Moon, Seung-Hyeon Royal Society of Chemistry 2008 Journal of environmental monitoring Vol.10 No.5
<P>A highly sensitive enzyme electrode was prepared based on gold nanoparticles for measurement of pesticides. Gold nanoparticles of 25–30 nm were synthesized on a glassy carbon electrode by double-pulse technique while the coverage was controlled by applied potential and time. The gold nanoparticles were modified to form a self-assembled monolayer, followed by covalent binding of tyrosinase. The TYR-AuNP-GC electrode was compared with bare GC, AuNP-GC, and modified AuNP-GC and TYR-Au (plate type) electrodes in terms of cyclic voltammetry. The voltammograms well represent the sensitivity of enzymatic oxidation of catechol, substrates for the enzyme activity. The prepared electrode integrated into a continuous flow system and was tested to detect pesticides, such as 2,4-D, atrazine, and ziram. Under the optimized conditions of the flow system, the electrode performed reasonably according to the inhibition mechanism in the concentration range of 0.001–0.5 ng mL<SUP>−1</SUP>. The enhanced performance was attributed to the favored microenvironment for the enzyme activity provided by SAM on gold nanoparticles.</P> <P>Graphic Abstract</P><P>A highly sensitive enzyme electrode using gold nanoparticles was prepared and its feasibility in on-line monitoring of pesticides at the ppt level was demonstrated. <IMG SRC='http://pubs.rsc.org/services/images/RSCpubs.ePlatform.Service.FreeContent.ImageService.svc/ImageService/image/GA?id=b800553b'> </P>