• 제목/요약/키워드: H%27

검색결과 6,259건 처리시간 0.042초

Isolation of Alcohol-tolerant Amylolytic Saccharomyces cerevisiae and Its Application to Alcohol Fermentation

  • Jung, He-Kyoung;Park, Chi-Duck;Bae, Dong-Ho;Hong, Joo-Heon
    • Food Science and Biotechnology
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    • 제17권6호
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    • pp.1160-1164
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    • 2008
  • An novel amylolytic yeast, Saccharomyces cerevisiae HA 27, isolated from nuruk, displayed resistance against high sugar (50% glucose) and alcohol (15%). Maximal production of amylolytic enzyme by S. cerevisiae HA 27 was achieved on 9 days of cultivation at the optimal temperature $20^{\circ}C$ and pH 6.0. The activity of amylolytic enzyme produced by S. cerevisiae HA 27 was stable, even at $70^{\circ}C$, and over a broad pH range (4.0-11.0). Also, the amylolytic enzyme of S. cerevisiae HA 27 showed optimal activity in pH 5.0 at $50^{\circ}C$. S. cerevisiae HA 27 exhibited 6.2%(v/v) alcohol fermentation ability using starch as a carbon source.

Helicobacter pylori에 감염된 위상피세포에서 Skp2의 변화 (Changes in Skp2 in Helicobacter pylori-Infected Gastric Epithelial Cells)

  • 정혜연
    • 한국식품영양학회지
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    • 제25권1호
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    • pp.64-68
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    • 2012
  • It has been suggested that Helicobacter pylori(H. pylori) infections can promote the development and progression of gastric cancer through the modulation of cell cycle regulators such as $p27^{Kip1}$ and Skp2. $p27^{Kip1}$ is a cyclin-dependent kinase (CDK) inhibitor that blocks the G1/S transition necessary for cell cycle progression. Skp2 is a component of the ubiquitin ligase complex called $SCF^{Skp2}$(SKP1-Cullin-F-box), which specifically binds and promotes the degradation of $p27^{Kip1}$. A low level of $p27^{Kip1}$ and a high level of Skp2 have been reported in many types of cancers, including gastric cancer. In addition, a decrease in $p27^{Kip1}$ has been reported in H. pylori-infected specimens. However, data on Skp2 in H. pylori infections are limited. This study examines the changes in the status of Skp2 in H. pylori-infected gastric epithelial AGS cells. For this, we stimulated AGS cells with H. pylori(NCTC 11637) at the ratio of 300:1(bacterium:cell) for 6 hours. The results of an immunoprecipitation analysis, followed by a western blot, indicate that the interaction between Skp2 and 14-3-3 was elevated 3 hours after the H. pylori treatment. In addition, there was an increase in cytoplasmic Skp2 after 3 hours, whereas there was no change in the nuclear level. Since it has been reported that interaction with 14-3-3 and the subsequent cytoplasmic translocation of Skp2 can increase its protein stability, increases in the interaction with 14-3-3 and the cytoplasmic Skp2 after the H. pylori treatment can increase the level of Skp2 in AGS cells. This phenomenon may explain, at least to some extent, the mechanism underlying the relationship between H. pylori infections and gastric carcinogenesis.

Preparation of 125

  • Kim, Byoung-Soo;Kim, Eun-Jung;Lee, Hae-June;Han, Sang-Jin;Choi, Tae-Hyun;Lee, Yun-Sil;Cheon, Gi-Jeong
    • Bulletin of the Korean Chemical Society
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    • 제31권9호
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    • pp.2649-2655
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    • 2010
  • $PKC{\delta}$-catalytic V5 Heptapeptide (FEQFLDI, FP7) interacts with heat shock protein 27 (HSP27) and inhibits HSP27-mediated resistance to cell death against various stimuli including radiation therapy. Here, we prepared radio-iodinated heptapeptide and further investigated its uptake properties in HSP27 expression cells. Peptide sequence of FP7 and a negative control peptide (WSLLEKR, QP7) was modified by substituting their C-terminus residue to tyrosine (FP6Y and QP6Y) to label radio-iodine. Iodinated peptides were confirmed by LC mass analysis with cold iodine reaction mixture. Accumulation of [$^{125}I$]iodo-FP6Y and [$^{125}I$]iodo-QP6Y in NCI-H1299 cell line, with higher level of HSP27, and NCI-H460 cell line, with lower level of HSP27, was measured by NaI(Tl) scintillation counter. The modification of substituting C-terminus residue of FP7 to tyrosine (FP6Y) did not affect its interaction with HSP27. Accumulation of [$^{125}I$]iodo-FP6Y in NCI-H1299 cells was 3 fold higher than in NCI-H460 cells. The novel radio-iodinated FP6Y would be used as a tracer for targeting HSP27 protein.

Direct characterization of E2-dependent target specificity and processivity using an artificial p27-linker-E2 ubiquitination system

  • Ryu, Kyoung-Seok;Choi, Yun-Seok;Ko, Jun-Sang;Kim, Seong-Ock;Kim, Hyun-Jung;Cheong, Hae-Kap;Jeon, Young-Ho;Choi, Byong-Seok;Cheong, Chae-Joon
    • BMB Reports
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    • 제41권12호
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    • pp.852-857
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    • 2008
  • Little attention has been paid to the specificity between E2 and the target protein during ubiquitination, although RING-E3 induces a potential intra-molecular reaction by mediating the direct transfer of ubiquitin from E2 to the target protein. We have constructed artificial E2 fusion proteins in which a target protein (p27) is tethered to one of six E2s via a flexible linker. Interestingly, only three E2s (UbcH5b, hHR6b, and Cdc34) are able to ubiquitinate p27 via an intra-molecular reaction in this system. Although the first ubiquitination of p27 (p27-Ub) by Cdc34 is less efficient than that of UbcH5b and hHR6b, the additional ubiquitin attachment to p27-Ub by Cdc34 is highly efficient. The E2 core of Cdc34 provides specificity to p27, and the residues 184-196 are required for possessive ubiquitination by Cdc34. We demonstrate direct E2 specificity for p27 and also show that differential ubiquitin linkages can be dependent on E2 alone.

Characterization of a Novel Monoclonal Antibody (27H2) Recognizing Human CD34 Class III Epitope

  • Hong, Kwon-Pyo;Kang, Sung-Hee;Lee, Kyoung-Mee;Ji, Gil-Yong;Yoon, Sang-Soon;Kim, Jong-Suk;Son, Bo-Ra;Lee, Dong-Geun;Lee, Ok-Jun;Song, Hyung-Geun
    • IMMUNE NETWORK
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    • 제10권6호
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    • pp.239-246
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    • 2010
  • Background: Monoclonal antibodies (mAbs) recognizing Class III epitope of CD34 are essential for flow cytometric diagnosis of leukemia. Methods: 27H2 mAb was developed from a mouse alternatively immunized with human acute leukemia cell lines, KG1 and Molm-1. Using flow cytometric analysis of various leukemic cell lines and peripheral blood, immunohistochemical study of frozen tonsil, we characterized 27H2 mAb. Antigen immunoprecipitated with 27H2 mAb immunobloted with anti-CD34 mAb. A case of bone marrow sample of acute lymphoblastic leukemia (ALL) patient was obtained at CBNU Hospital. For epitope identification enzyme treatment with neuraminidase and O-sialoglycoprotein endopeptidase (OSGE) and blocking assay with known classIII mAb (HPCA-2) were done. Results: Only KG1 and Molm-1 revealed positive immunoreactivity. Immunohistochemical staining disclosed strong membranous immunoreactivity on high endothelial venules. Antigen immunoprecipitated by 27H2 mAb showed approximately 100 kDa sized band immunoblotted with anti-CD34 under non-reducing conditions. Epitope recognized by 27H2 mAb disclosed resistancy to both neuraminidase and OSGE treatment and completely blocked with known class III mAb preincubation. CD34 positive leukemic cells in BM of pre B cell ALL patient detected by FITC-conjugated 27H2 and HPCA-2 were identified with similar sensitivity. Conclusion: A novel murine mAb recognizing class III epitope of human CD34 with high affinity, which is useful for flow cytometric diagnosis of leukemia, was developed.

O3에 의한 아조염료 Acid Red 27의 산화분해시 구조 변화에 관한 연구 (Studies on the Oxidative Structural Change of Azo Dye Acid Red 27 by Ozone)

  • 백미화;김동수
    • 한국물환경학회지
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    • 제21권6호
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    • pp.564-568
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    • 2005
  • The structural change of azo dye (Acid Red 27) by oxidation with ozone has been investigated using FT-IR and $^1H$ NMR. The solution pH was observed to decrease during oxidation reaction, which was considered to be due to the generation of several organic and inorganic acids as the result of the decomposition of azo compound. The FT-IR analysis showed that changes of specific absorption bands of Acid Red 27 were observed after ozonation. When azo dye was oxidized by ozone, several new peaks were shown to appear by $^1H$ NMR analysis and the peaks were generally shifted to the direction of up field. This was presumably due to the breakage of benzene ring contained in the molecular structure of Acid Red 27 by the oxidation and the shape of peaks was shown to change according to the reaction time.