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      • Pyrolysis kinetics and thermal degradation characteristics of the pre-treated municipal sewage sludge by biophysical processing

        ( Rong Han ),( Jin-wen Liu ),( Hong-tao Wang ),( Yuan-cheng Zhang ) 한국폐기물자원순환학회 2011 ISWA Vol.2011 No.0

        Pyrolysis of municipal sewage sludge (MSS) is a promising thermal conversion technology for waste disposal and energy recycle. The product yield pattern of thermal degradation process is strongly relevant to the chemical composition of MSS. In the present study, MSS was firstly processed in a biophysical conversion reactor to adjust the moisture content and biomass fraction. The pyrolysis characteristics of products from biophysical pre-treatment were investigated using thermogravimetric analysis(TGA) and differential scanning calorimetry(DSC), with the materials decomposing between 30℃ to 900℃ at heating rates of 10, 20, 40 ℃/min. According to DTG curves, the kinetic model was performed according to a combination of five-step decomposition. The approximate composition of samples can be determined by each step due to its pyrolysis feature. The nth-order kinetic equations was utilized to describe component degradations and the apparent activation energies were calculated at 25.46, 14.48, 48.15, 85.22, 60.16 kJ/mol through Coats-Redfern integral method. The first-step decomposition was related to low stability organic compounds that derived from the intermediate products of metabolism. The other four steps are mostly ascribed to the non-biodegradable components. The product gas was detected on-line by mass spectrograph (MS) coupled with TGA, indicating the thermal degradation characteristics of various components in the pre-treated sample.

      • Comparative Study of Protein Profile during Development of Mouse Placenta

        Rong Xun Han,Hong Rye Kim,Kenji Naruse,Su Min Choi,Baek-Chul Kim,Chang Sik Park,Dong Il Jin 한국동물번식학회 2007 Reproductive & developmental biology Vol.31 No.4

        To examine the differential protein expression pattern in the 11.5 day post-coitus (dpc) and 18.5 dpc placenta of mouse, we have used the global proteomics approach by 2-D gel electrophoresis (2-DE) and MALDI-TOF-MS. The differential protein patterns of 3 placentae at the 11.5 dpc and 18.5 dpc from nature mating mice were analyzed. Proteins within isoelectric point range of 3.0~10.0, separately were analyzed in 2DE with 3 replications of each sample. A total of approximately 1,600 spots were detected in placental 2-D gel stained with Coomassie-blue. In the comparison of 11.5 dpc and 18.5 dpc placentae, a total of 108 spots were identified as differentially expressed proteins, of which 51 spots were up-regulated proteins such as alpha-fetoprotein, mKIAA0635 protein and transferrin, annexin A5, while 48 spots were down-regulated proteins such as Pre-B-cell colony-enhancing factor 1(PBEF), aldolase 1, A isoform, while 4 spots were 11.5 dpc specific proteins such as chaperonin and Acidic ribosomal phosphoprotein P0, while 3 spots were 18.5 dpc specific proteins such as aldo-keto reductase family 1, member B7 and CAST1/ERC2 splicing variant-1. Most identified proteins in this analysis appeared to be related with catabolism, cell growth, metabolism and regulation. Our results revealed composite profiles of key proteins involved in mouse placenta during pregnancy.

      • Protein Analysis of Porcine Oocytes Differentially Expressed in Mature Oocyte and Parthenogentic Embryo

        Rong Xun Han,Yun Fei Diao,Hong Rye Kim,Min Gu Lee,Dong Il Jin 한국동물번식학회 2012 Reproductive & Developmental Biology(Supplement) Vol.36 No.2s

        An understanding of oocyte gene expression is a necessary for the study of early female gamete development. Recently, oocyte has been used in many techniques such as somatic cell nuclear transfer, intracytoplasmic sperm injection and embryonic stem cell derivation. The purpose of this study was to investigate in the proteomes of pig oocytes and identification of differential proteins between using DIGE technique. In this experiment to overcome of limitation of 2D gel method like a low reproducibility and low sensitivity for proteome analysis of very small quantities, 2D fluorescence difference gel electrophoresis (DIGE), which enables co-detection of up to three samples on the same 2DE gels with CyDyes was used for analysis of oocyte proteins. Proteins within an isoelectric point (pI) range of 3 to 10 and a molecular weight (Mw) range of 20~100 kDa were primarily analyzed in DIGE with 2 replications of each sample. Approximately 1000 spots were detected in 2-D gel. Then, image analysis of DeCyder was performed to detect variations in protein spots between mature oocyte and parthenogenesis embryo. In the comparison of mature oocyte and parthenogenesis embryo, 11 spots were identified to be up-regulated proteins and 2 spots to be down-regulated proteins in parthenogenesis embryo, among which proteins were zona pellucida glycoprotein 4, transferrin receptor, apolipoprotein B, L-3-Hydroxyacyl Coa Dehydrogenase Revisited, cytochrome P450 2C33, similar to Monocarboxylate transporter 2, 2'-5' oligoadenylate synthetase 3, interferon alpha/ beta receptor-1, Chloride channel protein 6, pyruvate carboxylase as well as2'-5' oligoadenylate synthetase 3 using MALDI-TOF-MS. These results suggested that differential proteins were present between mature oocyte and parthenogenesis embryo.

      • Identification of Bovine Pregnancy-Specific Whey Proteins using Two-Dimensional Gel Electrophoresis

        Han, Rong-Xun,Choi, Su-Min,Kim, Myung-Youn,Quan, Yan Shi,Kim, Baek-Chul,Diao, Yun Fei,Koqani, Reza,Park, Chang-Sik,Jin, Dong-Il The Korean Society of Animal Reproduction 2008 Reproductive & developmental biology Vol.32 No.4

        The early diagnosis of bovine pregnancy is an essential component of successful reproductive planning on farms, because lack of bovine pregnancy over the long term results in reproductive failure and low milk yield-the latter of which is a special concern on dairy farms. This study was designed to identify early pregnancy-specific whey proteins in bovine, by comparing milk samples collected from cattle during pregnancy (Days 30 and 50) and from non-pregnant cattle. In this study, differentially expressed proteins in five pregnant and five non-pregnant Holstein dairy cattle were investigated and compared, using proteomics analysis. The first dimension was applied to a pH $3.0{\sim}10.0$ strip, by loading a 2-mg milk protein sample. After the second-dimension separation was performed, the gels were stained with colloidal Coomassie brilliant blue. The stained gels were scanned and the images were analyzed, to detect variations in protein spots between non-pregnant and pregnant cattle milk protein spots, using ImageMaster, this was followed by analysis with MALDI TOF-MS. Analysis of the 2-DE gel image resulted in a total of approximately $500{\sim}600$ protein spots, of which 12 spots were differentially expressed, six spots were up-regulated, and four spots were down-regulated; two spots were identified as pregnancy-specific proteins. These proteins were identified as lactoferrin, NA-DH dehydrogenase subunit 2, albumin, serum albumin precursor and transferrin. Our results via 2-D PAGE analysis revealed composite profiles of several milk proteins related to early bovine pregnancy, implying the possible use of these milk proteins in the early detection of bovine pregnancy.

      • A Comparative Study of Protein Profiles in Porcine Fetus Fibroblast Cells with Different Confluence States

        Han, Rong-Xun,Kim, Hong-Rye,Diao, Yunfei,Kim, Myung-Youn,Park, Chang-Sik,Jin, Dong-Il The Korean Society of Animal Reproduction 2009 Reproductive & developmental biology Vol.33 No.4

        To examine the differential expression of proteins during the cycling (70~80% confluences) and G0/G1 (full confluences) phases in porcine fetal fibroblast cells, we used a global proteomics approach by 2-D gel electrophoresis (2-DE) and MALDI-TOF-MS. Cycling cell were harvested at approximately 70% to 80% confluent state while cells in G0/G1 phase were recovered after maintenance of a confluent state for 48 hr. Cellular proteins with isoelectric points ranging between 3.0~10.0, were analyzed by 2-DE with 2 replicates of each sample. A total of approximately 700 spots were detected by 2.D gels stained with Coomassie brilliant blue. On comparing the cell samples obtained from the cycling and G0/G1 phases, a total of 13 spots were identified as differentially expressed proteins, of which 8 spots were up-regulated in the cycling cell and 5 were up-regulated in the G0/G1 phase. Differentially expressed proteins included K3 keratin, similar to serine protease 23 precursor, protein disulfide-isomerase A3, microsomal protease ER-60, alpha-actinin-2, and heat-shock protein 90 beta. The identified proteins were grouped on the basis of their basic functions such as molecular binding, catabolic, cell growth, and transcription regulatory proteins. Our results show expression profiles of key proteins in porcine fetal fibroblast cells during different cell cycle status.

      • Induction of Apoptosis by IGFBP3 Overexpression in Hepatocellular Carcinoma Cells

        Han, Jian-Jun,Xue, De-Wen,Han, Qiu-Rong,Liang, Xiao-Hong,Xie, Li,Li, Sheng,Wu, Hui-Yong,Song, Bao Asian Pacific Journal of Cancer Prevention 2014 Asian Pacific journal of cancer prevention Vol.15 No.23

        Background: The insulin-like growth factor (IGF) system comprises a group of proteins that play key roles in regulating cell growth, differentiation, and apoptosis in a variety of cellular systems. The aim of this study was to investigate the role of insulin-like growth factor binding protein 3 (IGFBP3) in hepatocellular carcinoma. Materials and Methods: Expression of IGF2, IGFBP3, and PTEN was analyzed by qRT-PCR. Lentivirus vectors were used to overexpress IGFBP3 in hepatocellular carcinoma cell (HCC) lines. The effect of IGFBP3 on proliferation was investigated by MTT and colony formation assays. Results: Expression of IGF2, IGFBP3, and PTEN in several HCC cell lines was lower than in normal cell lines. After 5-aza-2'-deoxycytidine/trichostatin A treatment, significant demethylation of the promoter region of IGFBP3 was observed in HCC cells. Overexpression of IGFBP3 induced apoptosis and reduced colony formation in HUH7 cells. Conclusions: Expression of IGF2, IGFBP3, and PTEN in several HCC cell lines was lower than in normal cell lines. After 5-aza-2'-deoxycytidine/trichostatin A treatment, significant demethylation of the promoter region of IGFBP3 was observed in HCC cells. Overexpression of IGFBP3 induced apoptosis and reduced colony formation in HUH7 cells.

      • KCI등재

        Identification of Bovine Pregnancy-Specific Whey Proteins using Two-Dimensional Gel Electrophoresis

        Rong Xun Han,Su Min Choi,Myung Youn Kim,Yan Shi Quan,Baek-Chul Kim,Yun Fei Diao,Reza Koqani,Chang Sik Park,Dong Il Jin 한국동물생명공학회(구 한국동물번식학회) 2008 Reproductive & developmental biology Vol.32 No.4

        The early diagnosis of bovine pregnancy is an essential component of successful reproductive planning on farms, because lack of bovine pregnancy over the long term results in reproductive failure and low milk yield‐the latter of which is a special concern on dairy farms. This study was designed to identify early pregnancy‐specific whey proteins in bovine, by comparing milk samples collected from cattle during pregnancy (Days 30 and 50) and from non‐pregnant cattle. In this study, differentially expressed proteins in five pregnant and five non‐pregnant Holstein dairy cattle were investigated and compared, using proteomics analysis. The first dimension was applied to a pH 3.0~10.0 strip, by loading a 2‐mg milk protein sample. After the second‐dimension separation was performed, the gels were stained with colloidal Coomassie brilliant blue. The stained gels were scanned and the images were analyzed, to detect variations in protein spots between non‐pregnant and pregnant cattle milk protein spots, using ImageMaster; this was followed by analysis with MALDI TOF‐MS. Analysis of the 2‐DE gel image resulted in a total of approximately 500~600 protein spots, of which 12 spots were differentially expressed, six spots were up‐regulated, and four spots were downregulated; two spots were identified as pregnancy‐specific proteins. These proteins were identified as lactoferrin, NADH dehydrogenase subunit 2, albumin, serum albumin precursor and transferrin. Our results via 2‐D PAGE analysis revealed composite profiles of several milk proteins related to early bovine pregnancy, implying the possible use of these milk proteins in the early detection of bovine pregnancy.

      • Effects of Carbon Formation on Catalytic Performance for CO<sub>2</sub> Reforming with Methane on Ni/Al<sub>2</sub>O<sub>3</sub> Catalyst: Comparison of Fixed-Bed with Fluidized-Bed Reactors

        Han, Young Kyu,Ahn, Chang-Il,Bae, Jong-Wook,Kim, A Rong,Han, Gui Young American Chemical Society 2013 INDUSTRIAL & ENGINEERING CHEMISTRY RESEARCH - Vol.52 No.37

        <P>The amount of carbon formed and the H<SUB>2</SUB>/CO molar ratio for the carbon dioxide reforming (CDR) reaction with methane were investigated on Ni/Al<SUB>2</SUB>O<SUB>3</SUB> catalyst using a laboratory-scale fixed-bed reactor and a bench-scale fluidized-bed reactor. A significant suppression of carbon deposition in the fluidized-bed reactor compared with the fixed-bed reactor can be mainly induced from different product gas flow patterns by the continuous circulation of catalysts in oxidizing and reducing regions. This approach also enhances the gasification rate of deposited carbon in an expanded catalyst bed by increasing the amount of water adsorbed. The higher H<SUB>2</SUB>/CO ratio above 1.0 in the fluidized-bed reactor is also attributed to the enhanced gasification rate of deposited carbon precursors. The differences in the conversions of CH<SUB>4</SUB> and CO<SUB>2</SUB> and the H<SUB>2</SUB>/CO ratios in the two reactors are responsible for the different competitive rates of the reverse water–gas shift (RWGS) reaction, the Boudouard reaction, and the gasification of carbon precursors.</P><P><A href='http://pubs.acs.org/doi/suppl/10.1021/ie3028558'>ACS Electronic Supporting Info</A></P>

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