• Title/Summary/Keyword: Anion binding

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DNA Binding Studies and Cytotoxicity of the Novel 1,10-phenanthroline Palladium(II) Complexes of Dithiocarbamate Derivatives (디티오카르바메이트 유도체의 새로운 1,10-페난트롤린 팔라디움(II) 착물의 DNA 결합 성질 및 세포독성에 관한 연구)

  • Mansouri-Torshizi, Hassan;Saeidifar, Maryam;Ghasemi, Zahra Yekke;Khastan, Mahmood;Divsalar, Adeleh;Saboury, Ali Akbar
    • Journal of the Korean Chemical Society
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    • v.55 no.1
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    • pp.70-80
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    • 2011
  • Two new palladium (II) complexes, [Pd (phen)(pip-dtc)]$NO_3$ and [Pd(phen)(mor-dtc)]$NO_3$, (where phen is 1,10-Phenantroline, pip-dtc is piperidinedithiocarbamate anion and mor-dtc is morpholinedithiocarbamate anion) have been synthesized and characterized by elemental analysis, spectroscopic studies (FT-IR, $^1H$ NMR, UV-Vis) and conductance measurement. In these complexes, the dithiocarbamate ligands coordinate with Pd (II) center as bidentate with two sulfur atoms. These two complexes have been tested against chronic myelogenous leukemia cell line, K562. They show $IC_{50}$ values less than cisplatin and thus the mode of binding of the complexes to calf thymus DNA (CT-DNA) were investigated by ultraviolet difference and fluorescence spectroscopy. They can denature DNA, exhibit cooperative binding and intercalate into DNA. Several binding and thermodynamic parameters are also described.

Consensus channelome of dinoflagellates revealed by transcriptomic analysis sheds light on their physiology

  • Pozdnyakov, Ilya;Matantseva, Olga;Skarlato, Sergei
    • ALGAE
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    • v.36 no.4
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    • pp.315-326
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    • 2021
  • Ion channels are membrane protein complexes mediating passive ion flux across the cell membranes. Every organism has a certain set of ion channels that define its physiology. Dinoflagellates are ecologically important microorganisms characterized by effective physiological adaptability, which backs up their massive proliferations that often result in harmful blooms (red tides). In this study, we used a bioinformatics approach to identify homologs of known ion channels that belong to 36 ion channel families. We demonstrated that the versatility of the dinoflagellate physiology is underpinned by a high diversity of ion channels including homologs of animal and plant proteins, as well as channels unique to protists. The analysis of 27 transcriptomes allowed reconstructing a consensus ion channel repertoire (channelome) of dinoflagellates including the members of 31 ion channel families: inwardly-rectifying potassium channels, two-pore domain potassium channels, voltage-gated potassium channels (Kv), tandem Kv, cyclic nucleotide-binding domain-containing channels (CNBD), tandem CNBD, eukaryotic ionotropic glutamate receptors, large-conductance calcium-activated potassium channels, intermediate/small-conductance calcium-activated potassium channels, eukaryotic single-domain voltage-gated cation channels, transient receptor potential channels, two-pore domain calcium channels, four-domain voltage-gated cation channels, cation and anion Cys-loop receptors, small-conductivity mechanosensitive channels, large-conductivity mechanosensitive channels, voltage-gated proton channels, inositole-1,4,5-trisphosphate receptors, slow anion channels, aluminum-activated malate transporters and quick anion channels, mitochondrial calcium uniporters, voltage-dependent anion channels, vesicular chloride channels, ionotropic purinergic receptors, animal volage-insensitive cation channels, channelrhodopsins, bestrophins, voltage-gated chloride channels H+/Cl- exchangers, plant calcium-permeable mechanosensitive channels, and trimeric intracellular cation channels. Overall, dinoflagellates represent cells able to respond to physical and chemical stimuli utilizing a wide range of G-protein coupled receptors- and Ca2+-dependent signaling pathways. The applied approach not only shed light on the ion channel set in dinoflagellates, but also provided the information on possible molecular mechanisms underlying vital cellular processes dependent on the ion transport.

PROTEIN-CROSS-LINKING BY METHYLGLYOXAL

  • Lee, Cheolju;Kang, Sa-Ouk
    • Proceedings of the Korean Biophysical Society Conference
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    • 1996.07a
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    • pp.46-46
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    • 1996
  • To elucidate the mechanism for the cross-linking reaction in the glycation or Maillard reaction, we studied the reaction between proteins, and a three-carbon ${\alpha}$-ketoaldehyde, methylglyoxal. When Cu, Zn-SOD was incubated with 200 mM of methylglyoxal, the peroxidase activity as well as the superoxide dismutase activity was reduced. This reduction is accompanied by the decrease of the anion binding affinity of the enzyme. (omitted)

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Effects of DIDS on single $Ca^{2+}$ release channel behavior of skeletal muscle

  • Seo, In-Ra;Kim, Do-Han
    • Proceedings of the Korean Biophysical Society Conference
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    • 2001.06a
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    • pp.46-46
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    • 2001
  • Evidence has suggested that an anion channel blocker, 4, 4'-diisothiocyanatostilbene-2, 2' disulfonic acid (DIDS) could trigger Ca release from skeletal sarcoplasmic reticulum (SR) by binding to a 30 kDa SR protein. Since the high molecular weight $Ca^{2+}$ release channel (CRC)/ryanodine receptor (RyR) is the main SR protein that conducts $Ca^{2+}$ efflux in skeletal muscles, the relationship between CRC and the 30kDa protein remains to be elucidated.(omitted)

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Electron Paramagnetic Resonance Study of Bis(N-methyl-2-amino-1-cyclopentenedithiocarboxylato)Copper (II)

  • Woo-Seong Kim;Young-Inn Kim;Sung-Nak Choi
    • Bulletin of the Korean Chemical Society
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    • v.11 no.2
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    • pp.85-88
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    • 1990
  • The electron paramagnetic resonance (EPR) spectrum of the copper (II) complex with the 2-methylamino-1-cyclo-pentene-1-dithiocarboxylate (acdc) anion, $Cu(N-CH_3acdc)_2$ has been studied in the diamagnetic host lattices afforded by the corresponding divalent nickel, zinc, cadmium and mercury complexes. EPR parameters of the complex support the exclusive use of sulfur atoms by the ligand in metal binding. A combination of host lattice structure and covalency effects can be account for the observed spin-Hamiltonian parameters.

Band Electronic Structure Study of Two-Dimensional Organic Metal (BEDT-TTF)2Cu5I6 with a Polymer Anion Layer

  • Dae Bok Kang
    • Bulletin of the Korean Chemical Society
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    • v.12 no.5
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    • pp.515-517
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    • 1991
  • The electronic behavior of a organic metal $(BEDT-TTE)_2$${Cu_5}{I_6}$ observed to be stable at low temperatures was examined by performing tight-binding band electronic structure calculations. The suppression of a metal-insulator tansition is likely to originate from its quasi-two-dimensional Fermi surface with no nesting, in agreement with experiment.

Calix[4]pyrroles Bearing Pyrene-pickets at Diametrical Meso-positions with Amide Linkage

  • Yoo, Jae-Duk;Park, In-Won;Kim, Tae-Young;Lee, Chang-Hee
    • Bulletin of the Korean Chemical Society
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    • v.31 no.3
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    • pp.630-634
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    • 2010
  • The synthesis and ion binding properties of calix[4]pyrrole bearing pyrene moieties appended to one side of the calix[4]pyrrole are reported. The key feature is the presence of flexible fluorescence arms attached to the calix[4]pyrrole ring in a cis-fashion. The preliminary solution phase anion and cation binding studies revealed that the systems can be in fact as viable sensors for anionic guest.

Expession of the Recombinant Klebsiella aerognes UreF Protein as a MalE Fusion

  • Kim, Keun-Young;Yang, Chae-Ha;Lee, Mann-Hyung
    • Archives of Pharmacal Research
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    • v.22 no.3
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    • pp.274-278
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    • 1999
  • Expression of the active urease of the enterobacterium, Klebsiella aerogens, requires the presence of the accessory genes (ureD, ureE, ureF, and ureG) in addition to the three structural genes (ureA, ureB, and ureC). These accessory genes are involved in functional assembly of the nickel-metallocenter for the enzyme. Characterization of ureF gene has been hindered, however, since the UreF protein is produced in only minute amount compared to other urease gene products. In order to overexpress the ureF gene, a recombinant pMAL-UreF plasmid was constructed from which the UreF was produced as a fusion with maltose-binding protein. The MBP-UreF fusion protein was purified by using an amylose-affinity column chromatography followed by an anion exchange column chromatography. Polyclonal antibodies raised against the fusion protein were purified and shown to specifically recognize both MBP and UreF peptides. The UreF protein was shown to be unstable when separated from MBP by digestion with factor Xa.

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Isolation of calcium-binding peptides from porcine meat and bone meal and mussel protein hydrolysates (돼지 육골분 및 진주담치 단백질의 가수분해물 제조 및 칼슘 결합 물질의 분리)

  • Jung, Seung Hun;Song, Kyung Bin
    • Food Science and Preservation
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    • v.22 no.2
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    • pp.297-302
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    • 2015
  • Calcium is one of the essential mineral for the humans due to its crucial physiological functions in the body. Calcium deficiency results in many diseases, such as osteoporosis. Therefore, calcium supplements are available as a functional food. However, most calcium supplements in the market have a limitation due to poor absorption and low bioavailability. Thus, calcium-chelated peptides for improving the absorption rate of calcium have been isolated from foods including porcine meat and bone meal (MBM), and mussel using the enzymatic hydrolysis of their protein. The hydrolysates of food were ultra-filtered in order to obtain small peptides less than 3 kDa and the Ca-binding peptides were isolated via the anion exchange chromatography. The binding activity and concentration of Ca-binding pepetides were determined. In particular, the MBM and mussel protein hydrolysates were fractionated by mono Q and Q-Sepharose, respectively. As a result, among the fractions, the fractions of MBM F2 and mussel F3 showed the highest Ca-binding activity. These results suggest that MBM and mussel protein hydrolysates can be used as calcium supplements.