• 제목/요약/키워드: Monomeric species

검색결과 42건 처리시간 0.025초

Potentially Multidentate Tripodal Amine Catechol Ligands as Chelators for Ga(III) and In(III)

  • Sahoo, Suban K.;Baral, Minati;Bera, Rati Kanta;Kanungo, B. K.
    • Bulletin of the Korean Chemical Society
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    • 제30권9호
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    • pp.1956-1962
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    • 2009
  • The binding abilities of two multidentate tripodal amine catechol ligands, cis,cis-1,3,5-tris[(2,3-dihydroxybenzylamino) aminomethyl]cyclohexane (TMACHCAT, $L^1)\;and\;N^1,N^3,N^5$-tris(2-(2,3-dihydroxybenzylamino) ethyl)cyclohexane-1,3,5-tricarboxamide (CYCOENCAT, $L^2$) with Ga(III) and In(III) have been investigated by potentiometric and spectrophotometric methods in an aqueous medium of 0.1 M KCl at 25 ${\pm}\;1\;{^{\circ}C}.$ The ligands $L^1\;and\;L^2$ formed various monomeric species $MLH_3,\;MLH_2$, MLH and ML (M = $Ga^{+3}\;and\;In^{+3}$) and showed potential to form strong encapsulated tris(catechol) type complexes. The coordination modes, binding ability and selectivity of the ligands towards Ga(III) and In(III) have been discussed with the help of experimental evidences, and supported with molecular modeling calculations.

제조방법에 따른 NH3-SCR용 V/TiO2의 구조적 특성 제어 및 반응활성 영향 연구 (A Study of Structural Characteristic Control and Reaction Activity of V/TiO2 for NH3-SCR according to Preparation Method)

  • 신중훈;권동욱;홍성창
    • 한국대기환경학회지
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    • 제33권4호
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    • pp.297-305
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    • 2017
  • In this study, the activity and structural properties of catalysts prepared by mechanochemical method under dry condition were studied. A dry milling was used as a mechanochemical method. The precursors of vanadium were $NH_4VO_3$ and $V_2O_5$. The activity and characterization of the catalysts prepared by dry milling were compared with those prepared by impregnation. In addition, the correlation between the catalytic activity and the structural characteristics was observed through XRD, Raman, and $H_2$-TPR analysis. As a result, the monomeric vanadate species exhibited excellent redox characteristics, which were confirmed to be related to the catalytic activity.

Molecular characterization of a lectin, BPL-4, from the marine green alga Bryopsis plumosa (Chlorophyta)

  • Han, Jong-Won;Yoon, Kang-Sup;Jung, Min-Gui;Chah, Kyong-Hwa;Kim, Gwang-Hoon
    • ALGAE
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    • 제27권1호
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    • pp.55-62
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    • 2012
  • A novel lectin specific to N-acetyl-D-galactosamine as well as N-acetyl-D-glucosamine was isolated from Bryopsis plumosa and named as BPL-4. Sodium dodecyl sulfate polyacrylamide gel electrophorese (SDS-PAGE) and matrix-assisted laser desorption / ionization-time of flight (MALDI-TOF) mass spectrometry data showed that this lectin was a monomeric protein with molecular weight 12.9 kDa. The N-terminal amino acid sequences of the lectin were determined by Edman degradation and the full cDNA sequence encoding this lectin was obtained using the degenerate primers designed from the amino acid sequence. The size of the cDNA was 414 bp containing single open reading frame (ORF) encoding the lectin precursor. The homology analysis showed that this lectin might belong to H lectin group. BPL-4 showed high sequence similarity (60.6%) to BPL-3, which is a previously reported lectin from the same species. The comparative analysis on the lectin's primary structure showed two conserved domains including one possible active domain of H lectin group.

Purification and Properties of Intracellular Invertase from Alkalophilic and Thermophilic Bacillus cereus TA-11

  • Yoon, Min-Ho;Choi, Woo-Young;Kwon, Su-Jin;Yi, Sung-Hun;Lee, Dae-Hyung;Lee, Jong-Soo
    • Journal of Applied Biological Chemistry
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    • 제50권4호
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    • pp.196-201
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    • 2007
  • An intracellular invertase was purified to homogeneity from the cell extract of an alkalophilic and thermophilic Bacillus sp. TA-11, which was classified as a new species belonging to Bacillus cereus based on chemotaxanomic and phylogenetic analyses. The purified enzyme with a recovery of 26.6% was determined to be a monomeric protein with a molecular weight of 23 kDa by SDS-PAGE and 26 kDa by gel filtration. The maximum enzyme activity was observed at pH 7.0 and $50^{\circ}C$, and the purified enzyme was stable at the pH range of 5.0 to 8.0 and below $60^{\circ}C$. $K_m$ and $V_{max}$ values of the enzyme for sucrose were 370 mM and 3.0 ${\mu}M$ per min, respectively. The enzyme activity was significantly inhibited by bivalent metal ions ($Hg^{2+}$, $Cd^{2+}$ and $Cu^{2+}$) and sugars (glucose and fructose).

천연 밀단백질/계면활성제 복합체의 세정에 있어 피부보호 (The Cutaneous Protection for Detergent Formulation of Nature Wheat Protein Surfactant Complexes)

  • 정환경;박흥조;김명수;남기대
    • 한국응용과학기술학회지
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    • 제19권2호
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    • pp.79-85
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    • 2002
  • The cutaneous tolerability of detergent formulations can be improved by means of suitable additives. They complex the surfactant molecules lowering the concentration of their free monomeric species. Proteins derivatives used as additives for detergency are usually prepared by partial hydrolysis of plant reserve proteins. The main purpose of the hydrolytic cleavage is to make them water soluble and suitable for liquid products. Water solubility and stability are obtained by means of complexation with surfactants which also increase their actual hydrophobicity, an important parameter affecting cosmetic properties of proteins. Transepidermal water loss (TEWL) and electric capacitance (EC) have been adopted as investigation technigues to evaluate the skin integrity/damage in vitro tests, The performance of native wheat protein / surfactant complexes has been compared with traditional protein hydrolysates as detergent additives. The results show a noticeable reduction of skin irritation in surfactant formulations with addition of native wheat protein.

The effect of Glomus intraradices on the physiological properties of Panax ginseng and on rhizospheric microbial diversity

  • Tian, Lei;Shi, Shaohua;Ma, Lina;Zhou, Xue;Luo, Shasha;Zhang, Jianfeng;Lu, Baohui;Tian, Chunjie
    • Journal of Ginseng Research
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    • 제43권1호
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    • pp.77-85
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    • 2019
  • Background: Glomus intraradices is a species of arbuscular mycorrhizal fungi that, as an obligate endomycorrhiza, can form mutually beneficial associations with plants. Panax ginseng is a popular traditional Chinese medicine; however, problems associated with ginseng planting, such as pesticide residues, reduce the ginseng quality. Methods: In this experiment, we studied the effect of inoculating G. intraradices on several physiological properties and microbial communities of ginseng. UV-Visible Spectrum method was used to detect physical properties. Denaturing gradient gel electrophoresis method was used to analyze microbial communities. Results: The results indicated that inoculation with G. intraradices can improve the colonization rate of lateral ginseng roots, increase the levels of monomeric and total ginsenosides, and improve root activity as well as polyphenol oxidase and catalase activities. We also studied the bacterial and fungal communities in ginseng rhizospheric soil. In our study, G. intraradices inoculation improved the abundance and Shannon diversity of bacteria, whereas fungi showed a reciprocal effect. Furthermore, we found that G. intraradices inoculation might increase some beneficial bacterial species and decreased pathogenic fungi in rhizospheric soil of ginseng. Conclusion: Our results showed that G. intraradices can benefit ginseng planting which may have some instructive and practical significance for planting ginseng in farmland.

Physiological Effects of GLT1 Modulation in Saccharomyces cerevisiae Strains Growing on Different Nitrogen Sources

  • Brambilla, Marco;Manuela Adamo, Giusy;Frascotti, Gianni;Porro, Danilo;Branduardi, Paola
    • Journal of Microbiology and Biotechnology
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    • 제26권2호
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    • pp.326-336
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    • 2016
  • Saccharomyces cerevisiae is one of the most employed cell factories for the production of bioproducts. Although monomeric hexose sugars constitute the preferential carbon source, this yeast can grow on a wide variety of nitrogen sources that are catabolized through central nitrogen metabolism (CNM). To evaluate the effects of internal perturbations on nitrogen utilization, we characterized strains deleted or overexpressed in GLT1, encoding for one of the key enzymes of the CNM node, the glutamate synthase. These strains, together with the parental strain as control, have been cultivated in minimal medium formulated with ammonium sulfate, glutamate, or glutamine as nitrogen source. Growth kinetics, together with the determination of protein content, viability, and reactive oxygen species (ROS) accumulation at the single cell level, revealed that GLT1 modulations do not significantly influence the cellular physiology, whereas the nitrogen source does. As important exceptions, GLT1 deletion negatively affected the scavenging activity of glutamate against ROS accumulation, when cells were treated with H2O2, whereas Glt1p overproduction led to lower viability in glutamine medium. Overall, this confirms the robustness of the CNM node against internal perturbations, but, at the same time, highlights its plasticity in respect to the environment. Considering that side-stream protein-rich waste materials are emerging as substrates to be used in an integrated biorefinery, these results underline the importance of preliminarily evaluating the best nitrogen source not only for media formulation, but also for the overall economics of the process.

Bi-flavonoids are Superior to Mono-flavonoid in Inhibiting Amyloid-${\beta}$ Toxicity and Fibrillogenesis through Accumulating Nontoxic Oligomer-like Structures

  • Merlin Jayalal, L.P.
    • 통합자연과학논문집
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    • 제5권2호
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    • pp.107-119
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    • 2012
  • Polymerization of monomeric amyloid-${\beta}$ peptides ($A{\beta}$) into soluble oligomers and insoluble fibrils is one of the major pathways triggering the pathogenesis of Alzheimer's disease (AD). Using small molecules to prevent the polymerization of $A{\beta}$ peptides can, therefore, be an effective therapeutic strategy for AD. In this study, we investigated the effects of mono- and bi-flavonoids on $A{\beta}42$ toxicity and fibrillogenesis and found that the bi-flavonoid, taiwaniaflavone (TF) effectively and specifically inhibits $A{\beta}$ toxicity and fibrillogenesis. Compared to TF, the mono-flavonoid apigenin (AP) is less effective and less specific. Our data showed that differential effects of the mono- and bi-flavonoids on $A{\beta}$ fibrillogenesis correlate with their varying cytoprotective efficacies. We also found that other bi-flavonoids, namely 2',8"-biapigenin, amentoflavone, and sumaflavone, can also effectively inhibit $A{\beta}$ toxicity and fibrillogenesis, implying that the participation of two mono-flavonoids in a single bi-flavonoid molecule enhanced their activity. Bi-flavonoids, while strongly inhibited $A{\beta}$ fibrillogenesis, accumulated nontoxic $A{\beta}$ oligomeric structures, suggesting that these are off-pathway-oligomers. Moreover, TF abrogated the toxicity of preformed $A{\beta}$ oligomers and fibrils, indicating that TF and other bi-flavonoids may also reduce the toxicity of toxic $A{\beta}$ species. Altogether, our data clearly show that bi-flavonoids, possibly due to the possession of two $A{\beta}$ binders separated by an appropriate size linker, are likely to be promising therapeutics to suppress $A{\beta}$ toxicity.

Dimethyldodecylamine Oxide 의 물/n-프로판올 용매에서 혼합미셸 형성에 관한 열역학적 연구 (Thermodynamics on the Mixed Micellar Formation of Dimethyldodecylamine Oxide in Water/n-Propanol)

  • 이병환
    • 대한화학회지
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    • 제37권6호
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    • pp.562-569
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    • 1993
  • Dimethyldodecylamine Oxide(DDAO)의 미셀화에 대한 pH 효과와 n-프로판올 효과를 조사하기위하여 유사상태분리모델(pseudophase separation model)을 이용하였다. DDAO는 양성자화된 양이온 계면활성제와 비산성화된 중성 계면활성제 두 종류로 존재할 수 있으며, 이들은 열역학적으로 이성분 혼합메셀을 형성할 수 있다. 각 성분의 조성은 용액의 pH에 따라 달라지며, 각 종류 계면활성제들의 활동도, 미셀상태의 조성, 단량체상태의 조성 및 pH에 따른 임계미셀농도를 유사상태분리이론을 이용하여 실험적인 DDAO의 적정곡선으로부터 계산하였다. 임계미셀농도와 DDAO의 산-염기 해리평형상수($K_a$)는 미셀상태의 조성에 따라 변하였으며, 이들은 pH가 5인 지점에서 최소점 현상을 보이고 있다. 그리고 n-프로판올을 첨가하므로써 DDAO의 임계미셀농도는 감소하였으며, n-프로판올의 농도가 증가할수록 임계미셀농도는 더욱 감소하였다.

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A New Esterase, Belonging to Hormone-Sensitive Lipase Family, Cloned from Rheinheimera sp. Isolated from Industrial Effluent

  • Virk, Antar Puneet;Sharma, Prince;Capalash, Neena
    • Journal of Microbiology and Biotechnology
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    • 제21권7호
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    • pp.667-674
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    • 2011
  • The gene for esterase (rEst1) was isolated from a new species of genus Rheinheimera by functional screening of E. coli cells transformed with the pSMART/HaeIII genomic library. E. coli cells harboring the esterase gene insert could grow and produce clear halo zones on tributyrin agar. The rEst1 ORF consisted of 1,029 bp, corresponding to 342 amino acid residues with a molecular mass of 37 kDa. The signal P program 3.0 revealed the presence of a signal peptide of 25 amino acids. Esterase activity, however, was associated with a homotrimeric form of molecular mass 95 kDa and not with the monomeric form. The deduced amino acid sequence showed only 54% sequence identity with the closest lipase from Cellvibrio japonicus strain Ueda 107. Conserved domain search and multiple sequence alignment revealed the presence of an esterase/ lipase conserved domain consisting of a GXSXG motif, HGGG motif (oxyanion hole) and HGF motif, typical of the class IV hormone sensitive lipase family. On the basis of the sequence comparison with known esterases/ lipases, REst1 represents a new esterase belonging to the class IV family. The purified enzyme worked optimally at $50^{\circ}C$ and pH 8, utilized pNP esters of short chain lengths, and showed best catalytic activity with p-nitrophenyl butyrate ($C_4$), indicating that it was an esterase. The enzyme was completely inhibited by PMSF and DEPC and showed moderate organotolerance.