Metal Ion-Dependent Fluorescent Dynamics of Photoexcited Zinc−Porphyrin and Zinc−Myoglobin Modified with Ethylenediaminetetraacetic Acid

2008 ◽  
Vol 112 (48) ◽  
pp. 15493-15502 ◽  
Author(s):  
Hiroshi Takashima ◽  
Hiroe Kawahara ◽  
Miho Kitano ◽  
Satomi Shibata ◽  
Hiroshi Murakami ◽  
...  
Keyword(s):  
Metal Ion ◽  
Ethylenediaminetetraacetic Acid ◽  
Zinc Porphyrin ◽  
Zinc Myoglobin

scholarly journals Characterization of Endolysin LyJH307 with Antimicrobial Activity against Streptococcus bovis

Animals ◽  
2020 ◽  
Vol 10 (6) ◽  
pp. 963 ◽  
Author(s):  
Hanbeen Kim ◽  
Hyo Gun Lee ◽  
Inhyuk Kwon ◽  
Jakyeom Seo
Keyword(s):  
Metal Ion ◽  
Modular Design ◽  
Ethylenediaminetetraacetic Acid ◽  
Streptococcus Bovis ◽  
Cell Wall Binding ◽  
Zoocin A ◽  
Alkaline Conditions ◽  
A Cell ◽  
Cell Wall Binding Domain

Streptococcus bovis (S. bovis) is one of the critical initiators of acute acidosis in ruminants. Therefore, we aimed to develop and characterize the endolysin LyJH307, which can lyse ruminal S. bovis. We tested the bactericidal activity of recombinant LyJH307 against S. bovis JB1 under a range of pH, temperature, NaCl, and metal ion concentrations. In silico analyses showed that LyJH307 has a modular design with a distinct, enzymatically active domain of the NLPC/P60 superfamily at the N-terminal and a cell wall binding domain of the Zoocin A target recognition domain (Zoocin A_TRD) superfamily at the C-terminal. The lytic activity of LyJH307 against S. bovis JB1 was the highest at pH 5.5, and relatively higher under acidic, than under alkaline conditions. LyJH307 activity was also the highest at 39 °C, but was maintained between 25°C and 55°C. LyJH307 bactericidal action was retained under 0-500 mM NaCl. While the activity of LyJH307 significantly decreased on treatment with ethylenediaminetetraacetic acid (EDTA), it was only restored with supplementation of 10 mM Ca2+. Analyses of antimicrobial spectra showed that LyJH307 lysed Lancefield groups D (S. bovis group and Enterococcus faecalis) and H (S. sanguinis) bacteria. Thus, LyJH307 might help to prevent acute ruminal acidosis.

Control of Zn, Cu and Mn activities in alkaline and calcareous soils equilibrated with EDTA

1982 ◽  
Vol 98 (1) ◽  
pp. 203-207 ◽  
Author(s):  
S. P. Singh
Keyword(s):  
Metal Ion ◽  
Ethylenediaminetetraacetic Acid ◽  
Ph Dependence ◽  
Calcareous Soils ◽  
Transition Metal Ions ◽  
Ion Activities ◽  
Solid Phases ◽  
Equilibrium Mole Fraction ◽  
Edta Ethylenediaminetetraacetic Acid

SUMMARYThe modified EDTA (ethylenediaminetetraacetic acid) method of determining the ionic activities in soils developed by Norvell was used to measure Zn2+, Cu2+ and Mn2+ activities including the competition of Ca and Mg for the chelating ligand EDTA. In the Zn-EDTA system, the equilibrium mole fraction of CaL2− + MgL2− increased with an increase in pH of the soil solution, thereby leading to a decrease in the concentration of transition metal ions. In view of the pH dependence of the metal ion activities, the values of the expression pM + 2 pOH (where M may be Zn, Cu or Mn) were used to discuss the possible role of various oxides, hydroxides, carbonates, sulphides and unknown solid phases in regulating the activities of Zn2+, Cu2+ and Mn2+ ions in alkaline and calcareous soils.

scholarly journals Ts2631 Endolysin from the Extremophilic Thermus scotoductus Bacteriophage vB_Tsc2631 as an Antimicrobial Agent against Gram-Negative Multidrug-Resistant Bacteria

Viruses ◽  
2019 ◽  
Vol 11 (7) ◽  
pp. 657 ◽  
Author(s):  
Magdalena Plotka ◽  
Malgorzata Kapusta ◽  
Sebastian Dorawa ◽  
Anna-Karina Kaczorowska ◽  
Tadeusz Kaczorowski
Keyword(s):  
Metal Ion ◽  
Ethylenediaminetetraacetic Acid ◽  
Bacterial Load ◽  
Multidrug Resistant ◽  
Resistant Bacteria ◽  
Gram Negative ◽  
Log Reduction ◽  
Carbapenem Resistant ◽  
Heat Stable ◽  
Transmission Electron

Bacteria that thrive in extreme conditions and the bacteriophages that infect them are sources of valuable enzymes resistant to denaturation at high temperatures. Many of these heat-stable proteins are useful for biotechnological applications; nevertheless, none have been utilized as antibacterial agents. Here, we demonstrate the bactericidal potential of Ts2631 endolysin from the extremophilic bacteriophage vB_Tsc2631, which infects Thermus scotoductus, against the alarming multidrug-resistant clinical strains of Acinetobacter baumannii, Pseudomonas aeruginosa and pathogens from the Enterobacteriaceae family. A 2–3.7 log reduction in the bacterial load was observed in antibacterial tests against A. baumannii and P. aeruginosa after 1.5 h. The Ts2631 activity was further enhanced by ethylenediaminetetraacetic acid (EDTA), a metal ion chelator (4.2 log reduction in carbapenem-resistant A. baumannii) and, to a lesser extent, by malic acid and citric acid (2.9 and 3.3 log reductions, respectively). The EDTA/Ts2631 combination reduced all pathogens of the Enterobacteriaceae family, particularly multidrug-resistant Citrobacter braakii, to levels below the detection limit (>6 log); these results indicate that Ts2631 endolysin could be useful to combat Gram-negative pathogens. The investigation of A. baumannii cells treated with Ts2631 endolysin variants under transmission electron and fluorescence microscopy demonstrates that the intrinsic antibacterial activity of Ts2631 endolysin is dependent on the presence of its N-terminal tail.

Biological characteristics of recombinant enhancin ofTrichoplusia nigranulovirus expressed inEscherichia coli

2006 ◽  
Vol 3 (3) ◽  
pp. 171-176
Author(s):  
Yuan Zhe-Ming ◽  
Meng Xiao-Lin ◽  
Liu Shu-Sheng
Keyword(s):  
Trichoplusia Ni ◽  
Metal Ion ◽  
Inclusion Bodies ◽  
Ethylenediaminetetraacetic Acid ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Biological Characteristics ◽  
Cotton Bollworm ◽  
Peritrophic Membrane

AbstractA recombinant enhancin fromTrichoplusia nigranulovirus, expressed inEscherichia coliand named P96, had been shown in a previous study to increase significantly the efficacy of bio-insecticides applied to insect pests. Here, several biological characteristics were clarified to provide further proof for the activities of P96. The inclusion bodies formed by P96 were quite stable when expressed inE. coli; however, they could be effectively dissolved in sodium carbonate (Na2CO3) solution or in the midgut digestive secretion of the fifth-instar larvae of the cotton bollworm,Helicoverpa armigera,in vitro. According to sodium dodecyl sulphate–polyacrylamide gel electrophoresis (SDS-PAGE), the peritrophic membrane of the cotton bollworm was clearly decomposed by P96. With the increase of P96 concentration, the mortality of the cotton bollworm caused by nuclear polyhedrosis virus increased up to its saturation concentration, 6.76×105inclusion bodies/ml. The bioactivity of P96 was strongly inhibited by ethylenediaminetetraacetic acid (EDTA), which formed a complex compound with the metal ion (Zn2+) in the protein.

The effect of pH and ligands on the sorption of heavy metal ions by cellulose

1978 ◽  
Vol 31 (7) ◽  
pp. 1501 ◽  
Author(s):  
H Farrah ◽  
WF Pickering
Keyword(s):  
Metal Ions ◽  
Metal Ion ◽  
Ethylenediaminetetraacetic Acid ◽  
Zinc Ions ◽  
Natural Systems ◽  
Ph Values ◽  
Hydrated Ions ◽  
Pka Value ◽  
Anionic Complexes ◽  
Copper Lead

The adsorption of copper, lead, cadmium and zinc ions by cellulose suspensions has been examined at pH values ranging from 3.5 to 11. The chemical form of the metal ions has been changed by adding ligands such as oxalic acid, citric acid, tartaric acid, ethylenediaminetetraacetic acid, ethylene- diamine, glycine, cysteine and α,α'-bipyridyl. Stable anionic complexes were not sorbed by the cellulose, and at a given pH cationic complexes were sorbed less than hydrated ions. The presence of excess ligand generally served to mask the precipitation of the metal- hydroxy species which can occur in the pH 6-7 region. ��� The amount of metal cation sorbed increased with pH. This has been attributed to increased ionization of acid functional groups having a pKa value of around 4.4. ��� The implication of the results, in respect to aqueous metal ion levels in natural systems, has been considered.

scholarly journals Histidine-rich protein 2: a new pathogenic factor of Plasmodium falciparum malaria

2021 ◽  
Author(s):  
Takashi Iwasaki ◽  
Mayu Shimoda ◽  
Haru Kanayama ◽  
Tsuyoshi Kawano
Keyword(s):  
Plasmodium Falciparum ◽  
Malaria Infection ◽  
Metal Ion ◽  
Therapeutic Agent ◽  
Ethylenediaminetetraacetic Acid ◽  
Protozoan Parasite ◽  
Plasmodium Falciparum Malaria ◽  
Pathogenic Factor ◽  
Cell Penetration ◽  
Promising Candidate

Plasmodium falciparum causes serious malaria symptoms; when this protozoan parasite infects human erythrocytes, it produces and secretes large amounts of histidine–rich protein 2 (PfHRP2) into human blood. Thus, PfHRP2 is a well–known diagnostic marker for malaria infection. Here, however, we also identified PfHRP2 as a pathogenic factor produced by P. falciparum. PfHRP2 showed cell penetration and cytotoxicity against various human cells. In particular, PfHRP2 showed significant cytotoxicity over 5 days at the same concentration as in P. falciparum–infected patients′ blood (90–100 nM). This result is consistent with the mortality rate of P. falciparum malaria, which increases rapidly in untreated cases for 3–7 days. In addition, the cell penetration and cytotoxicity of PfHRP2 increased 2.5– and 2.6–fold, respectively, in the absence of serum, which suggests that low serum protein concentrations (occurring during malnutrition, for example) increase the risk of adverse effects from PfHRP2 (consistent with malnutrition increasing the lethality of malaria infection). We also showed that PfHRP2 bound to Ca2+ ions, localized to intracellular lysosomes, increased lysosomal Ca2+ levels, and inhibited the basal level of autophagy by inhibiting autolysosome formation. Furthermore, the Ca2+–dependent cytotoxicity of PfHRP2 was suppressed by the metal ion chelator ethylenediaminetetraacetic acid (EDTA). In summary, our findings suggest that PfHRP2 acts as a pathogenic factor in P. falciparum–infected patients and is associated with the exacerbation of malaria. Furthermore, EDTA is a promising candidate as a therapeutic agent for the suppression of PfHRP2 pathogenicity. Overall, this study provides new insights into P. falciparum malaria pathogenesis and treatment.

scholarly journals Mechanical homeostasis of a DOPA-enriched biological coating from mussels in response to metal variation

2015 ◽  
Vol 12 (110) ◽  
pp. 20150466 ◽  
Author(s):  
Clemens N. Z. Schmitt ◽  
Alette Winter ◽  
Luca Bertinetti ◽  
Admir Masic ◽  
Peter Strauch ◽  
...  
Keyword(s):  
Metal Ion ◽  
Ethylenediaminetetraacetic Acid ◽  
Local Environment ◽  
Natural Environments ◽  
Byssal Thread ◽  
Anthropogenic Inputs ◽  
Spatio Temporal ◽  
Mechanical Homeostasis ◽  
Fe Ions

Protein–metal coordination interactions were recently found to function as crucial mechanical cross-links in certain biological materials. Mussels, for example, use Fe ions from the local environment coordinated to DOPA-rich proteins to stiffen the protective cuticle of their anchoring byssal attachment threads. Bioavailability of metal ions in ocean habitats varies significantly owing to natural and anthropogenic inputs on both short and geological spatio-temporal scales leading to large variations in byssal thread metal composition; however, it is not clear how or if this affects thread performance. Here, we demonstrate that in natural environments mussels can opportunistically replace Fe ions in the DOPA coordination complex with V and Al. In vitro removal of the native DOPA–metal complexes with ethylenediaminetetraacetic acid and replacement with either Fe or V does not lead to statistically significant changes in cuticle performance, indicating that each metal ion is equally sufficient as a DOPA cross-linking agent, able to account for nearly 85% of the stiffness and hardness of the material. Notably, replacement with Al ions also leads to full recovery of stiffness, but only 82% recovery of hardness. These findings have important implications for the adaptability of this biological material in a dynamically changing and unpredictable habitat.

Cloning, Expression, and Purification of a Cu/Zn Superoxide Dismutase from Jatropha curcas

2013 ◽  
Vol 68 (1-2) ◽  
pp. 60-69
Author(s):  
Chao Ou-yang ◽  
Shun Gao ◽  
Feng Cai ◽  
Tsair-Wang Chung ◽  
Sheng-hua Wang ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Jatropha Curcas ◽  
Metal Ion ◽  
Ethylenediaminetetraacetic Acid ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Absorption Spectrometry ◽  
Reading Frame ◽  
Flight Mass Spectrometry ◽  
Ph Range

We report cDNA cloning, expression, purification, and characterization of a novel Cu/ Zn superoxide dismutase (SOD) from Jatropha curcas leaves. The full-length cDNA of this SOD contained a 496-bp open-reading frame (ORF) encoding 162 amino acid residues. The recombinant plasmid containing the SOD coding sequence was introduced into Escherichia coli, and the SOD was expressed as a fusion protein. The recombinant SOD was purified from a high-density fed-batch culture using a combination of immobilized metal ion affinity chromatography (IMAC) and Sephadex G25 desalting chromatography. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and matrix-assisted laser desorption/ ionization time-of-flight mass spectrometry (MALDI-TOF MS) analysis indicated that the recombinant SOD was a monomeric protein with a molecular mass of approximately 16.4 kDa. Isoelectric focusing showed that this SOD was a basic protein with pI values of 7.04, 7.33, 8.62, and 8.77. The activity of the SOD was stable at 70 °C for 10 min, and in a broad pH range from 4 to 9. The presence of urea (up to 8 M), guanidinium chloride (up to 6 M), and 2-mercaptoethanol (up to 8 mM) had little effect on the activity. The activity decreased gradually with increasing concentrations of imidazole, hydrogen peroxide, and ethylenediaminetetraacetic acid (EDTA). Atomic absorption spectrometry showed the presence of 0.239 copper and 0.258 zinc atoms, respectively, in the SOD polypeptide

Effects of ATP on lysosomes: inhibition of the loss of latency caused by cooling

1982 ◽  
Vol 242 (3) ◽  
pp. C192-C199 ◽  
Author(s):  
R. C. Ruth ◽  
W. B. Weglicki
Keyword(s):  
Metal Ion ◽  
Ethylenediaminetetraacetic Acid ◽  
Protective Action ◽  
Kinetic Studies ◽  
Protective Mechanism ◽  
Membrane Phase ◽  
Lysosomal Fraction ◽  
Divalent Metal Ion ◽  
Additional Loss

Triton-filled lysosomes from rat liver and a crude lysosomal fraction from livers of rats not injected with Triton have been used to study the ability of ATP to protect lysosomes against the effects of incubation in vitro at 37 degrees C. When incubation was carried out in a sucrose-NH4Cl medium at pH 8.0 or in buffer containing 0.15 M KCl at pH 7.4, ATP protected against the loss of lysosomal enzyme latency that occurred at 37 degrees C and also against the additional loss of latency that occurred when the incubated lysosomes were cooled to 0 degrees C. The inhibition of the effects of cooling was found to result from a decrease in the loss of latency caused specifically by cooling the lysosomes through the temperature range of the membrane phase transition (15-0 degrees C); ATP did not affect the basic rate of loss of latency at 0 degrees C. Protection was minimal when incubation was carried out in 1 mM ethylenediaminetetraacetic acid without added divalent metal ion and was enhanced by the addition of either Mg2+ or Ca2+. Kinetic studies were carried out on the ATP-protective action against the effects of cooling by adding ATP to lysosomes that had been incubated at 37 degrees C and that were then cooled to 0 degrees C at various times after addition of the ATP. Susceptibility to the effects of cooling continued to decrease until the ATP had been present at 37 degrees C for approximately 3 min before cooling. The concentration of ATP required for maximum initial rates of protection was found to be 10(-3) M or possibly lower. The rate of decrease in susceptibility to the effects of cooling was much slower when ATP was added at 22 than at 37 degrees C, suggesting that enzyme action may be involved in the protective mechanism. Possible mechanisms for the ATP-protective action are discussed.

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