RÉSUMÉ
This study explores the magnetic and magnetotransport behavior of polycrystalline ErAl3compound. The polycrystalline compound adopts HoAl3-type structures with the R-3m space group, No. 166-2 and hR60 configurations. Multiple magnetic orderings and two field-induced metamagnetic transitions are observed. ErAl3exhibits a significant magnetocaloric effect (MCE),-ΔSM= 15.25 J kg-1K-1and high relative cooling power of 383 J kg-1with applied magnetic field change (ΔH) of 70 kOe near the paramagnetic to ferromagnetic transition, showcasing its potential for magnetic refrigeration technology. The compound also demonstrates metallic behavior, with a notable magnetoresistance of 48.5%at 2 K due to the suppression of antiferromagnetism. The magnetic phase diagram reveals four distinct phases influenced by temperature and magnetic field, identified through the study of the MCE.
RÉSUMÉ
The magnetic and magnetocaloric properties of polycrystalline Gd0.5Sr0.5-xCaxMnO3 (x = 0.0, 0.2, 0.3, 0.4 and 0.5) compounds have been investigated. Depending upon the Ca and Sr proportions, fascinating magnetic ground states were observed in the Gd0.5Sr0.5-xCaxMnO3 compounds. Here, the dominating nature of the canted magnetic state (for the Gd0.5Ca0.5MnO3 compound) and glassy (disordered ferromagnetic) magnetic state (for the Gd0.5Sr0.5MnO3 compound) are observed. However, for the intermediate doped samples (x = 0.2, 0.3, 0.4), a competing nature is found in their magnetic and exchange bias properties. Additionally, in the low temperature region, a significantly large magnetocaloric effect is observed for all the samples. At a 70 kOe external magnetic field, the highest observed value of the magnetocaloric entropy change is 21.58 J kg-1 K-1 (for the Gd0.5Ca0.5MnO3 sample) and the lowest is 10.15 J kg-1 K-1 (for the Gd0.5Sr0.5MnO3 sample).
RÉSUMÉ
The detail investigations on the magneto-transport properties of the polycrystalline (Sm0.3Gd0.7)0.55Sr0.45MnO3(SGSMO-1) and (Sm0.5Gd0.5)0.55Sr0.45MnO3(SGSMO-2) compounds, having a glassy-like and ferromagnetic ground states respectively have been carried out in details. Due to the existence of two different magnetic ground states in the above mentioned systems, the magneto-transport properties are markedly differed from each other, specially at the low temperature region. The highly semi-conducting nature of the SGSMO-1 compound is suppressed with the application of magnetic field, whereas the SGSMO-2 compound exhibits a metal-insulator transition in its pristine state. The high-temperature semiconducting state of both the systems can be well-explained with the polaronic transport mechanisms via small-polaron hopping and variable-range-hopping models. The low-temperature metallic states for both the systems are explored by considering the various contributions arise from the grain boundary effect, electron-electron, electron-phonon, electron-magnon etc scattering processes. The spin-polarized tunneling transport mechanism at the grain boundaries plays a crucial role in the enhancement of low-field magnetoresistance in the studied systems.
RÉSUMÉ
Low-temperature-high-magnetic field magnetic force microscopy studies on colossal magnetoresistance material Sm0.5Ca0.25Sr0.25MnO3have been carried out. These measurements provide real-space visualization of antiferromagnetic-ferromagnetic (AFM-FM) transition on sub-micron length scale and explain the presence of AFM-FM transition in the temperature-dependent magnetization measurements, but the absence of corresponding metal-insulator transition in temperature-dependent resistivity measurements at the low magnetic field. Distribution of transition temperature over the scanned area indicates towards the quench disorder broadening of the first-order magnetic phase transition. It shows that the length scale of chemical inhomogeneity extends over several micrometers.
RÉSUMÉ
Cigarette smoking is a significant risk factor for cataract. However, the mechanism by which cigarette smoke (CS) causes cataract remains poorly understood. We had earlier shown that in CS-exposed guinea pig, p-benzoquinone (p-BQ) derived from CS in the lungs is carried by the circulatory system to distant organs and induces various smoke-related pathogeneses. Here, we observed that CS exposure caused accumulation of the p-BQ-protein adduct in the eye lens of guinea pigs. We also observed accumulation of the p-BQ-protein adduct in resected lens from human smokers with cataract. No such accumulation was observed in the lens of never smokers. p-BQ is a strong arylating agent that forms Michael adducts with serum albumin and haemoglobin resulting in alterations of structure and function. A major protein in the mammalian eye lens is αA-crystallin, which is a potent molecular chaperone. αA-crystallin plays a key role in maintaining the integrity and transparency of the lens. SDS-PAGE indicated that p-BQ induced aggregation of αA-crystallin. Various biophysical techniques including UV-vis spectroscopy, fluorescence spectroscopy, FT-IR, bis-ANS titration suggested a perturbation of structure and chaperone function of αA-crystallin upon p-BQ modification. Our results indicate that p-BQ is a causative agent involved in the modification of αA-crystallin and pathogenesis of CS-induced cataract. Our findings would educate public about the impacts of smoking on eye health and help to discourage them from smoking. The study might also help scientists to develop new drugs for the intervention of CS-induced cataract at an early stage.
Sujet(s)
Benzoquinones/toxicité , Cataracte/étiologie , Cataracte/métabolisme , Fumer des cigarettes/effets indésirables , Cristallines alpha/métabolisme , Sujet âgé , Animaux , Benzoquinones/composition chimique , Benzoquinones/pharmacocinétique , Benzoquinones/intoxication , Cataracte/induit chimiquement , Cataracte/anatomopathologie , Fumer des cigarettes/métabolisme , Fumer des cigarettes/anatomopathologie , Escherichia coli/génétique , Escherichia coli/métabolisme , Cochons d'Inde , Humains , Capsule du cristallin/effets des médicaments et des substances chimiques , Capsule du cristallin/métabolisme , Capsule du cristallin/anatomopathologie , Mâle , Adulte d'âge moyen , Chaperons moléculaires/métabolisme , Agrégation pathologique de protéines/induit chimiquement , Agrégation pathologique de protéines/métabolisme , Agrégation pathologique de protéines/anatomopathologie , Protéines recombinantes/biosynthèse , Protéines recombinantes/composition chimique , Protéines recombinantes/génétique , Cristallines alpha/biosynthèse , Cristallines alpha/composition chimique , Cristallines alpha/génétiqueRÉSUMÉ
In this work we have carried out an elaborate study on the magnetic properties and investigated the exchange bias phenomena of some charge-ordered (CO) manganites. The detailed study of Sm1-x Ca x MnO3 (x = 0.5, 0.55, 0.6, 0.65, 0.7) compounds shows that Sm0.4Ca0.6MnO3, which is the most robust charge ordered material studied here, shows significantly large exchange bias field (HE) as compared to the other compounds. Our experimental results and analysis indicate that TCO, which reflects the stability of the charge-ordered state, is one of the key parameters for the exchange bias effect. Similar behaviour is found in other rare-earth analogues, viz., La1-x Ca x MnO3 and Pr1-x Ca x MnO3 compounds as well. We also found that with increasing stability of CO states in Sm1-x Ca x MnO3 compounds, HE enhances due to increase in number and reduction in size of ferromagnetic clusters.
RÉSUMÉ
The Physics of materials with large magnetoresistance (MR), defined as the percentage change of electrical resistance with the application of external magnetic field, has been an active field of research for quite some times. In addition to the fundamental interest, large MR has widespread application that includes the field of magnetic field sensor technology. New materials with large MR is interesting. However it is more appealing to vast scientific community if a method describe to achieve many fold enhancement of MR of already known materials. Our study on several manganite samples [La(1-x)Ca(x)MnO3 (x = 0.52, 0.54, 0.55)] illustrates the method of significant enhancement of MR with the reduction of the particle size in nanometer scale. Our experimentally observed results are explained by considering model consisted of a charge ordered antiferromagnetic core and a shell having short range ferromagnetic correlation between the uncompensated surface spins in nanoscale regime. The ferromagnetic fractions obtained theoretically in the nanoparticles has been shown to be in the good agreement with the experimental results. The method of several orders of magnitude improvement of the magnetoresistive property will have enormous potential for magnetic field sensor technology.
RÉSUMÉ
Methylphophorbide a (MPa) has been isolated from the ethanol extract of the wheat grass plant. Its antioxidative efficacy is evaluated by hydroxyl radical scavenging activities and reducing capacity which are significantly up regulated in comparison with aqueous extract of the plant. The compound shows iron-binding capacity where the Fe(2+) binds with MPa by two types of binding patterns with dissociation constants 157.17 and 27.89. It has antioxidative and cytotoxic effects on HeLa and Hep G2 cells. The cancerous cell survivability decreases with increasing concentration of MPa. These findings have provided evidence for the traditional use of the wheat grass plant in the treatment of cancers, oxidative stress and iron overloaded disorders.
Sujet(s)
Antinéoplasiques d'origine végétale/pharmacologie , Antioxydants/pharmacologie , Chlorophylle/analogues et dérivés , Triticum/composition chimique , Apoptose/effets des médicaments et des substances chimiques , Chlorophylle/pharmacologie , Cellules HeLa , Cellules HepG2 , Humains , Stress oxydatif/effets des médicaments et des substances chimiques , Extraits de plantes/composition chimiqueRÉSUMÉ
DNA repair mechanisms are essential for the maintenance of genomic stability, proper cellular function and survival for all organisms. Plants, with their intrinsic immobility, are vastly exposed to a wide range of environmental agents and also endogenous processes which frequently cause damage to DNA and impose genotoxic stress. Therefore, in order to survive under frequent and extreme environmental stress conditions, plants have developed a vast array of efficient and powerful DNA damage repair mechanisms to ensure rapid and precise repair of genetic material for maintaining genome stability and faithful transfer of genetic information over generations. (1) Recently, we have defined the role of DNA polymerase λ in repair of UV-B-induced photoproducts in Arabidopsis thaliana via nucleotide excision repair pathway. (2) Here, we have further discussed potential function of DNA polymerase λ in various DNA repair pathways in higher plant genome in response to environmental and genotoxic stress factors.
Sujet(s)
Arabidopsis/génétique , Altération de l'ADN/génétique , DNA polymerase beta/métabolisme , Réparation de l'ADN , ADN des plantes , Génome végétal , Stress physiologique/génétique , Arabidopsis/enzymologie , Arabidopsis/métabolisme , DNA polymerase beta/génétique , Instabilité du génome , Rayons ultravioletsRÉSUMÉ
The transition and hysteresis widths of a disorder broadened first order magnetic transition vary in H-T space which influences the co-existing phase fraction at low temperature arising due to kinetic arrest of the first order transition. We explored the role of change in the relative width of the supercooling/superheating band and kinetic arrest band for a ferromagnetic metallic to antiferromagnetic insulating transition. It is shown that for a correlated kinetic arrest and supercooling bands, the topology of the devitrification curves (or transformation across the (H(K),T(K)) band during warming) changes with the change in the relative width of these two bands. In addition to this, for a broader kinetic arrest band, the transformation temperature across the superheating band under constant H now depends on the arrested phase fraction. These predictions have been tested on nanocrystalline Pr(0.67)Ca(0.33)MnO(3), which is known to show a large variation in hysteresis width in H-T space. This is the first report where correlation between the kinetic arrest band and the supercooling band has been shown experimentally, in contrast to the universal observation of anticorrelation reported so far.
RÉSUMÉ
BACKGROUND: Allium sativum leaf agglutinin (ASAL) is a 25-kDa homodimeric, insecticidal, mannose binding lectin whose subunits are assembled by the C-terminal exchange process. An attempt was made to convert dimeric ASAL into a monomeric form to correlate the relevance of quaternary association of subunits and their functional specificity. Using SWISS-MODEL program a stable monomer was designed by altering five amino acid residues near the C-terminus of ASAL. METHODOLOGY/PRINCIPAL FINDINGS: By introduction of 5 site-specific mutations (-DNSNN-), a ß turn was incorporated between the 11(th) and 12(th) ß strands of subunits of ASAL, resulting in a stable monomeric mutant ASAL (mASAL). mASAL was cloned and subsequently purified from a pMAL-c2X system. CD spectroscopic analysis confirmed the conservation of secondary structure in mASAL. Mannose binding assay confirmed that molecular mannose binds efficiently to both mASAL and ASAL. In contrast to ASAL, the hemagglutination activity of purified mASAL against rabbit erythrocytes was lost. An artificial diet bioassay of Lipaphis erysimi with mASAL displayed an insignificant level of insecticidal activity compared to ASAL. Fascinatingly, mASAL exhibited strong antifungal activity against the pathogenic fungi Fusarium oxysporum, Rhizoctonia solani and Alternaria brassicicola in a disc diffusion assay. A propidium iodide uptake assay suggested that the inhibitory activity of mASAL might be associated with the alteration of the membrane permeability of the fungus. Furthermore, a ligand blot assay of the membrane subproteome of R. solani with mASAL detected a glycoprotein receptor having interaction with mASAL. CONCLUSIONS/SIGNIFICANCE: Conversion of ASAL into a stable monomer resulted in antifungal activity. From an evolutionary aspect, these data implied that variable quaternary organization of lectins might be the outcome of defense-related adaptations to diverse situations in plants. Incorporation of mASAL into agronomically-important crops could be an alternative method to protect them from dramatic yield losses from pathogenic fungi in an effective manner.
Sujet(s)
Antifongiques/pharmacologie , Insecticides/pharmacologie , Lectines végétales/composition chimique , Lectines végétales/pharmacologie , Alternaria/effets des médicaments et des substances chimiques , Animaux , Antifongiques/composition chimique , Aphides/effets des médicaments et des substances chimiques , Technique de Western , Chromatographie d'affinité , Chromatographie sur gel , Fusarium/effets des médicaments et des substances chimiques , Ail/composition chimique , Insecticides/composition chimique , Mutagenèse dirigée , Feuilles de plante/composition chimique , Lectines végétales/génétique , Rhizoctonia/effets des médicaments et des substances chimiques , Spectrométrie de fluorescenceRÉSUMÉ
The purification and functional characterization of protein kinase A catalytic subunit (PKAcat) from bovine lens cytosol has been described. Purification to homogeneity has been achieved by using 100 kDa cut-off membrane filtration followed by Sephacryl S-300 chromatography and finally fractionating on High Q anion exchange column. The purified protein migrates as a single band of molecular mass approximately 41 kDa on 12.5% SDS-PAGE. Proteomic data from ion trap LC-MS when analyzed through NCBI blast program reveals significant homology (52%) with bovine zeta-crystallin and also some homology with pig casein kinase I alpha chain (38%) and SLA-DR1 beta 1 domain (38%). The search does not indicate homology with any known catalytic subunit of PKA. Inspite of the significant homology with the zeta-crystallin, our protein is different from it in terms of molecular mass. pI value of the kinase (5.3) obtained from 2D analysis is also different from zeta-crystallin (8.5). The protein is found to contain 17% alpha-helix, 26.5% beta-sheet, 21.4% turn and 34.7% random coil. The active catalytic subunit of the bovine lens cAMP-dependent kinase belongs to Type I Calpha subtype. The enzyme shows maximum activity at 30 min incubation in presence of 5 mM MgCl(2 )and 50 microM ATP. The kinase shows broad substrate specificity. It prefers Ser over Thr as phosphorylating residue. Phosphorylation of crystallin proteins, major protein fraction of bovine lens and phosphorylation of chaperone protein alpha crystallin by the kinase suggests that the kinase plays some crucial role in regulation of chaperone function within lens.