• Title/Summary/Keyword: B7H3

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$New η^3-Allyl-Alkenyl- and η^3-Allyl-Alkynyl-Ir-Cp^* Compounds from Reactions of [Cp^*Ir(η^3-CH_2CHCHPh)(NCMe)]^+ with Alkynes$

  • Jin, Jong Sik;Jong, Dae Seong;Kim, Mi Yeok;Lee, Hyeon Gwi
    • Bulletin of the Korean Chemical Society
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    • v.22 no.7
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    • pp.739-742
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    • 2001
  • Reactions of [Cp*Ir(η3-CH2CHCHPh)(NCMe)]OTf (1) with HC≡CR (R = H, CH2OH) in the presence of bases, B (B=NEt3, PPh3, AsPh3) produce stable Cp*Ir-η3-allyl-alkenyl compounds [Cp*Ir(η3-CH2CHCHPh)(-CH=CH-+B)]OTf (2) and [Cp*Ir(η3-CH2CHCHPh)(-C(CH2OH)=CH- +PPh3)]OTf (3), respectively in high yields. Cp*Ir-η3-allyl-alkynyl compounds Cp*Ir(η3-CH2CHCHPh(-C≡C-R') (4) and Cp*(η3-CH2CHCHPh)Ir-C≡C-p-C6H4-C≡C-Ir(η3-CH2CHCHPh)Cp* (5) have been prepared from reactions of 1 with HC≡CR'(R' = C6H5, p-C6H4CH3, C3H5, C6H9) and HC≡C-p-C6H4-C≡CH in the presence of NEt3.

Purification and Characterization of Lactate Dehydrogenase Isozymes in Channa argus (가물치(Channa argus) 젖산탈수소효소 동위효소들의 정제 및 특성)

  • Park, Eun-Mi;Yum, Jung-Joo
    • Journal of Life Science
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    • v.20 no.2
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    • pp.260-268
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    • 2010
  • The lactate dehydrogenase (EC 1.1.1.27, LDH) isozymes in tissues from Channa argus were purified and characterized by biochemical, immunochemical and kinetic methods. The activity of LDH in skeletal muscle was the highest at 380.4 units and those in heart, eye and brain tissues were 13.4, 3,5 and 5.4 units, respectively. Citrate synthase (EC 4.1.3.7, CS) activity in heart tissue was the highest at 20.7 units. LDH/CS in skeletal muscle, heart, eye and brain tissues were 172.9, 0.6, 0.32 and 0.47. Protein concentration in skeletal muscle tissue was 14.7 mg/g and specific activities of LDH in skeletal muscle, heart, eye and brain tissues were 25.88, 0.79, 0.31 and 1.38 units/mg, respectively. Therefore, skeletal muscle tissue was anaerobic and heart tissue was aerobic. The LDH isozymes in tissues were identified by polyacrylamide gel electrophoresis, immunoprecipitation and Western blot with antiserum against $A_4$, $B_4$, and eye-specific $C_4$. LDH $A_4$, $A_3B$, $A_2B_2$. $AB_3$ and $B_4$ isozymes were detected in every tissue, $C_4$, $AC_3$, $A_2C_2$ and $A_3C$ were detected in eye tissue, and $A_3C$ was found in brain tissue. LDH $A_4$, $A_3B$, $A_2B_2$, $AB_3$, $B_4$, eye-specific $C_4$ isozymes were purified by affinity chromatography and Preparative PAGE Cells. The LDH $A_4$ isozyme was purified in the fraction from elution with $NAD^+$ containing buffer of affinity chromatography. Eye-specific $C_4$ isozyme was eluted right after $A_4$, after which $B_4$ isozyme was eluted with plain buffer. As a result, one part of molecular structures in $A_4$, $B_4$ and eye-specific $C_4$ were similar, but were different from each other in $B_4$ and $C_4$. Therefore the subunit A may be conservative in evolution, and the evolution of subunit B seems to be faster than that of subunit A. The activity of LDH $A_4$, $A_2B_2$, $B_4$, and eye-specific $C_4$ isozymes remained at 39.98, 21.28, 19.67 and 16.87% as a result of the inhibition by 10 mM of pyruvate, so the degree of inhibition was very high. The $Km^{PYR}$ values were 0.17, 0.27 and 0.133 mM in $A_4$, $B_4$ and eye-specific $C_4$ isozymes, respectively. The optimum pH of LDH $A_4$, $B_4$, eye-specific $C_4$, $A_2B_2$, $A_3B$, and $AB_3$ were pH 6.5, pH 8.5, pH 5.5, pH 6.0-6.5, pH 5.0 and pH 7.5. The $A_4$ and heterotetramer isozymes stabilized a broad range of pH. Especially, LDH activities in skeletal muscle tissue were high, resulting in a high degree of muscle activity.LDH metabolism in eye tissue seems to be converted faster from pyruvate to lactate by eye-specific $C_4$ isozyme as eye-specific $C_4$ have the highest affinity for pyruvate, and right after the conversion, oxidation of lactate was induced by $A_4$ isozyme. It was found that expression of Ldh-C, affinity to substrate and reaction time of $C_4$ isozyme were different according to the ecological environmental and feeding capturing patterns.

$M\"{o}ssbauer$ studies of $NdFe_{10.7}TiM{0.3}(M\;=\;B,\;Ti)$ ($NdFe_{10.7}TiM{0.3}(M\;=\;B,\;Ti)$$M\"{o}ssbauer$ 연구)

  • 김철성;이용종;김윤배;김창석
    • Journal of the Korean Magnetics Society
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    • v.5 no.1
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    • pp.64-70
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    • 1995
  • The authors have studied crystallographic and magrletic properties of $NdFe_{10.7}TiM_{0.3}(M=B,\;Ti)$ by X-ray diffraction, VSM magnetometer, and Mossbauer spectrometer. The Alloys were prepared by arc-melting under argon atmosphere. The $NdFe_{10.7}TiM_{0.3}$ has pure single phase, whereas the $NdFe_{10.7}Ti_{1.3}$ contains some $\alpha-Fe$, from powder X-ray diffractometry. The $NdFe_{10.7}TiM_{0.3}$ has the $ThMn_{12}$-type tetragonal structure with $a_{0}=8.587\;{\AA}\;and\;c_{0}=4.788\;{\AA}$. The Curie temperature ($T_c$) is $570{\pm}3\;K$ from $M\"{o}ssbauer$ spectroscopy performed at various temperatures ranging from 13 to 770 K. Each spectrum of below $T_c$ was fitted with five subspectra of Fe sites in the structure ($8i_{1},\;8i_{2},\;8j_{1},\;8j_{2}\;and\;8f$). The area fraction of the subspectra at room temperature are 16.4, 8.2, 14.8, 21.3 and 39.3 %, respectively. Magenetic hyperfine fields for the Fe sites decrease in the order, $H_{hf}(8i)>H_{hf}(8j)>H_{hf}(8f)$.

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Media Optimization for the Production of Aminopeptidase M Inhibitors MR-387A and B by Streptomyces sp. SL-387 (Streptomyces sp. SL-387에 의한 Aminopeptidase M 저해제 MR-387A 및 B의 생산 배지 최적화)

  • Chung, Myung-Chul;Chun, Hyo-Kon;Lee, Ho-Jae;Lee, Choong-Hwan;Kim, Su-Il;Kho, Yung-Hee
    • Applied Biological Chemistry
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    • v.38 no.2
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    • pp.100-105
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    • 1995
  • Media optimization for the production of MR-387A and B, novel aminopeptidase M inhibitors by Streptomyces sp. SL-387 isolated from a soil was studied. Optimized medium was consisted of 1% glucose, 3% soybean meal, 0.2% yeast extract, 0.1% beef extract, 0.3% NaCl, 0.01% $K_2HPO_4$, 0.3% $CaCO_3$, 0.001% $MnCl_2{\cdot}4H_2O$, 0.001% $ZnCl_2{\cdot}7H_2O$, and 0.0005% $MgSO_4{\cdot}7H_2O$, and adjusted to pH 7.0 before autoclaving. When the optimized medium was used as a fermentation medium, maximum productivity of MR-387 was reached at 120 hours of fermentation, and total productivity was 909.1 U/ml.

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The hyaluronan synthesis inhibitor 7-hydroxy-4-methylcoumarin inhibits LPS-induced inflammatory response in RAW 264.7 macrophage cells

  • Kim, Gwan Bo;Hyun, Chang-Gu
    • Journal of Applied Biological Chemistry
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    • v.64 no.3
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    • pp.263-268
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    • 2021
  • 7-Hydroxy-4-methylcoumarin (7H-4MC) inhibits hyaluronan production in multiple cell lines and tissue types both in vitro and in vivo. It is a commercially available drug approved for human use, called hymecromone, in European and Asian countries to prevent biliary spasms. Nevertheless, as the pharmacological efficacy of 7H-4MC has not yet been reported in macrophages, this study investigated its anti-inflammatory effects and mechanism of action using lipopolysaccharide (LPS)-induced RAW 264.7 macrophages. LPS-induced RAW 264.7 cells were treated with various concentrations of 7H-4MC (62.5, 125, 250, and 500 μM). The application of 7H-4MC significantly reduced nitric oxide and prostaglandin E2 production without cytotoxic effects. Additionally, 7H-4MC strongly decreased the expression of inducible nitric oxide synthase and cyclooxygenase. Furthermore, 7H-4MC reduced the production of proinflammatory cytokines, such as tumor necrosis factor-α, interleukin (IL)-1β, and IL-6. Finally, 7H-4MC exerted its potent anti-inflammatory actions via the upregulation of IκB-α production, which led to the inhibition of nuclear factor-κB (NF-κB) activity. These results, obtained in macrophage cell lines, suggest that 7H-4MC prevents inflammatory diseases via the NF-κB signaling pathway and that its use could be beneficial for human health. Ultimately, this is the first report describing the anti-inflammatory activity of 7H-4MC in a macrophage cell line.

Synthesis of Cephalosporin Derivatives with Triazolylthiomethylpyrrolidines at the C-3 Side Chain (트리아조릴 티오메칠피로리딘을 3번 측쇄에 가진 세파로스포린 유도체의 합성)

  • 고옥현;홍준희
    • YAKHAK HOEJI
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    • v.46 no.5
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    • pp.313-319
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    • 2002
  • Synthesis of 7$\beta$-[(Z)-2-(2-aminothiazol-4-yl)-2-(1-carboxy-1-methylethoxyimino)acetamido]-3-[[(3S, 5S)-5-[4-phenyl-5-(4-methylphenyl or 2-thiophenyl)-4H-l, 2, 4- triazol-3-yl]thiomethylpyrrolidin-3-yl]]thiomethyl-3-cephem-4-carboxylic acids (7a, 7b) were described. (2S, 4S)-4-acethylthio-2-[4-phenyl-5-(4-methylphenyl or 2-thiophenyl)-4 H-1, 2, 4-triazol-3-yl]thiomethyl-1-tert-butoxycarbonylpyrrolidines (4a, 4b) were prepared from trans-4-hydroxy-L-proline with (2S, 4R)-absolute configuration as starting material. 4-Phenyl-5-(4-methylphenyl or 2-thiophenyl)-4 H-l, 2, 4-triazol-3-thiols (2a, 2b) were prepared from p-toluic anhydride and 2-thiophene carboxylic acid hydrazide, respectively. p-Methoxybenzyl 7$\beta$-(Z)-2-(2-for-mamidothiazol-4-yl)-2-(1-tert-butoxycarbonylisopropylimino]acetamido-3-[[ (3S, 5S)-5-[4-phenyl-5-(4-methylphenyl or 2-thio phenyl)-4H-1, 2, 3-triazol-3-yl]thiomethyl-1- tert-butoxycarbonylpyrrolidin-3-yl]]thiomethyl-3-cephem-4-carboxylates (6a, 6b) were achieved by using p-methoxybenzyl ]7P-(Z)-2-(2-formamidothiazol-4-yl)-2-(tert-butoxycarbonylisopropylimino] acetamido-3-chloromethyl-3-cephem-4-carboxylate (5) and (2S, 4S)-4-acethylthio-2-[4-phenyl-5-(4-methyl phenyl or 2-thiophenyl)-4H-1, 2, 4-triazol-3-yl]thiomethyl-1-tert-butoxycarbonyl pyrrolidines (4a, 4b). Removal of formyl, Boc, and p-methoxybenzyl protecting groups were carried out by triflu oroacetic acid and anisole to give the target compounds.

Studies on Enzyme of the the Thermophilic Mold (PartV.) Purification of Xylanase (고온성 사상균의 효소에 관한 연구 (제5보) Xylanase의 정제)

  • Kim, Kwan;Kim, Yang-Hee;Jung, Dong-Hyo
    • Microbiology and Biotechnology Letters
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    • v.2 no.3
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    • pp.133-140
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    • 1974
  • 1) Two xylanase (designed as A and B) of Myriococcus albomyces were purified from an extract of wheat koji culture. Puriscation steps included first ammonium sulfate fractionation followed successively by SE-Sephadex column chromatgraphy. DEAE-Sephadex column chromatography and gel filtration on Sephadex G-100 repectively. 2) The optimum pH and pH stability for crude xylanse were found to be pH 5.0 and pH 4.0-7.0 respectively. 3) The optimium temperature was found to he 5$0^{\circ}C$ and for the thermal statbility of xylanase, the enryme incubated at $65^{\circ}C$ for 60min did not affect their stability. 4) The purised xylanase A and B were considered as liquefying xylanase and saccharogenic xylauase repectively. 5) The Bylanase A was most active at pH 4.0 and range of pH 3.0-8.0 at 3$0^{\circ}C$ for six hrs. The B was most active at pH 5.0 showing stability range of pH 4.0 to 8.5 at 3$0^{\circ}C$ for 6 hrs. incubation respectively. The Optimum temperature of xylanase A and B were found to be 7$0^{\circ}C$ and $65^{\circ}C$ for 60min repectively.

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Crystallograpbic and Magnetic Properties of $Ni_{0.65}Zn_{0.35}Cu_{0.3}Fe_{1.7}O_4$ ($Ni_{0.65}Zn_{0.35}Cu_{0.3}Fe_{1.7}O_4$의 결정학적 및 자기적 특성 연구)

  • 김우철;김삼진;김철성;이승화
    • Journal of the Korean Magnetics Society
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    • v.9 no.3
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    • pp.136-142
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    • 1999
  • $Ni_{0.65}Zn_{0.35}Cu_{0.3}Fe_{1.7}O_4$ has been studied with x-ray diffraction, Mossbauer spectroscopy, and vibrating sample magnetometer. The crystal structure is found to be a cubic spinel with the lattice constant $a_0=8.403{\AA}$. Mossbauer spectra of have been taken at various temperatures ranging from 12 K to 665 K. as the temperature increases toward $T_N$ a systematic line broadening effect in the Mossbauer spectrum is observed and interpreted to originate from different temperature dependencies of the magenetic hyperfine fields at various iron sites. Also, by using binomial distribution equation we obtained the hyperfine fields of tetrahedral[A] and octahedral sites[B], $H_{hf}(A)=470\;kOe,\; H_{hf}(B0)=495 \;kOe,\; H_{hf}(B1)=485\;kOe, \;H_{hf}(B2)=453\;kOe,\; H_{hf}(B3)=424\;kOe,\; H_{hf}(B4)=390\;kOe,\; H_{hf}(Bavr)=451\;kOe$ respectively at room temperature. The isomer shift indicates that the iron ions are ferric at tetrahedral[A] and octahedral sites[B], respectively. The Neel temperature is determined to be $T_N=665\;K$. The results of the VSM data gave the magnetic moment and coercivity values of $M_S=66\; emu/g\;and\;H_C=36\;Oe$.

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Transcriptional repression of ANGPT1 by histone H3K9 demethylase KDM3B

  • Han, Arim;Chae, Yun-Cheol;Park, Jin Woo;Kim, Kee-Beom;Kim, Ji-Young;Seo, Sang-Beom
    • BMB Reports
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    • v.48 no.7
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    • pp.401-406
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    • 2015
  • Here we report that the H3K9 demethylase KDM3B represses transcription of the angiogenesis regulatory gene, ANGPT1. Negative regulation of ANGPT1 by KDM3B is independent of its Jumonji (JmjC) domain-mediated H3K9 demethylase activity. We demonstrate that KDM3B downregulates ANGPT1 via interaction with SMRT, and suggest that the repressor complex is formed at the promoter area of ANGPT1. Using MTT and wound healing assays, depletion of KDM3B was found to increase cell proliferation and cell motility, indicating that KDM3B has a role in angiogenesis. [BMB Reports 2015; 48(7): 401-406]