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  • 1
    Electronic Resource
    Electronic Resource
    Woodbury, NY : American Institute of Physics (AIP)
    Applied Physics Letters 80 (2002), S. 835-837 
    ISSN: 1077-3118
    Source: AIP Digital Archive
    Topics: Physics
    Notes: This letter reports the dielectric and ferroelectric properties of tungsten bronze Sr2−xCaxNaNb5O15 (SCNN, x=0.05–0.35) ceramics. Two dielectric anomalies and a diffuse ferroelectric transition behavior were appreciably observed in the compositions of x=0.05–0.25. The incorporation of smaller calcium cations into the crystal structure resulted in an increase in the Curie temperature, from 279 (x=0.05) to 297 (x=0.35), and a decrease in the permittivity, from 1353 to 543, at their respective Curie temperatures. Ferroelectricity was observed in the compositions with x=0.05–0.25, but absent in the compositions with x=0.30 and 0.35 at room temperature. The maximum spontaneous polarization Ps of 9.1 μC/cm2 and remanent polarization Pr of 3.0 μC/cm2 were achieved in the composition of x=0.15. © 2002 American Institute of Physics.
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  • 2
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 9 (1970), S. 4499-4504 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 12 (1973), S. 2862-2868 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
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  • 4
    Electronic Resource
    Electronic Resource
    Westerville, Ohio : American Ceramics Society
    Journal of the American Ceramic Society 85 (2002), S. 0 
    ISSN: 1551-2916
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Tungsten bronze Sr2−xCaxNaNb5O15 (SCNN, x= 0.1) piezoelectric ceramics were prepared by a novel super-fast sintering technique, i.e., spark plasma sintering (SPS). Sintering was conducted at temperatures ranging from 1000° to 1200°C under vacuum under 35 MPa. The heating rate varied from 30° to 300°C/min and the soaking time was in the range of 5 to 60 min. The microstructure and the phase identification were analyzed via scanning electron microscopy (SEM) and X-ray diffraction (XRD). The density of the sintered ceramics increased with an increase in sintering temperature as well as in heating rate. Materials with a near-theoretical density could be attained by sintering at 1200°C for 5 min with a heating rate of 300°C/min, exhibiting a homogeneous and fine-grained microstructure (grain size about 2.7 μm) and a uniform translucency. A tetragonal tungsten bronze phase was identified in ceramics sintered at temperatures above 1200°C, whereas the tungsten bronze phase transformed to a SrNb2O6-type phase in the materials sintered at temperatures below 1200°C. XRD patterns demonstrated a preferred crystallographic orientation of the SCNN grains with their c-axes perpendicular to the pressing direction.
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Plant molecular biology 20 (1992), S. 705-713 
    ISSN: 1573-5028
    Keywords: alanine aminotransferase ; C4 photosynthesis ; gene expression ; nucleotide sequencing ; Panicum miliaceum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have determined the nucleotide sequence of a cDNA encoding AlaAT-2, which is believed to function in the C4-pathway of Panicum miliaceum. An open reading frame (1446 bp) encodes a protein of 482 amino acid residues. The deduced amino acid sequence of AlaAT-2 shows 44.2 and 44.8% homology with the amino acid sequences of AlaATs from rat and human livers, respectively. Northern blot analysis showed that the gene encoding AlaAT-2 in mesophyll and bundle sheath cells was the same and transcribed similarly in the cells. The level of translatable mRNA for AlaAT-2 increased dramatically during greening.
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  • 6
    ISSN: 1573-5028
    Keywords: aspartate aminotransferase ; C4 photosynthesis ; gene expression ; gene structure ; isozyme
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The cytosolic and mitochondrial isozymes of aspartate aminotransferase (AspAT) function in the C4 photosynthetic cycle in NAD-malic enzyme-type C4 plants and are expressed at high levels in mesophyll cells and bundle sheath cells, respectively. We constructed a genomic library from Panicum miliaceum, a NAD-malic enzyme-type C4 plant, and cloned the genes for these isozymes. The sequence of the cloned gene for cytosolic AspAT spans 7800 bp and consists of 12 exons. The sequence of the cloned gene for mitochondrial AspAT spans 9000 bp and consists of 10 exons. The results of primer-extension analysis suggest that transcription may be initiated from multiple adjacent sites. Both genes have significant GC-rich regions around the site of initiation of transcription, and these regions showed no CpG suppression. The 5′-flanking regions of both genes include several short sequences similar to the regulatory elements found in other genes for components of the photosynthetic machinery. In particular, the cytosolic AspAT gene contains sequences similar to nuclear protein-binding sites in other mesophyll-expressed C4 photosynthetic genes and the mitochondrial AspAT gene contains elements for light-sensitive and constitutive expression of a bundle sheath-expressed gene. The results of Southern analysis indicated that there are at least two genes that encode each isozyme in the genome of P. miliaceum. A comparison of nitron-insertion positions between AspAT genes of plants and animals revealed that several introns are located at identical positions. On the basis of a phylogenetic tree among AspATs and tyrosine aminotransferase, we have shown that the introns of aminotransferase genes antedate the divergence of eubacteria, archaebacteria, and eukaryotes.
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  • 7
    ISSN: 1573-5028
    Keywords: 2-oxoglutarate/malate translocator ; C4 plant ; gene expression ; mitochondria ; Panicum miliaceum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Three cDNA clones that hybridize to a partial rice cDNA that show similarity to bovine mitochondrial 2-oxoglutarate/malate translocator were isolated from leaves of Panicum miliaceum L. (proso millet), an NAD-malic enzyme-type C4 plant. The nucleotide sequences of the clones resemble each other, and some of the isolated cDNAs contained extra sequences that seemed to be introns. The predicted proteins encoded by the cDNAs have 302 amino acids and molecular weights of 32211 and 32150. The hydrophobic profile of the amino acid sequence predicted the existence of six transmembrane α-helices that is a common property of members in the mitochondrial transporter family. The predicted amino acid sequence showed the highest similarity with that of the 2-oxoglutarate/malate translocator from mammalian mitochondria. An expression plasmid containing the coding region of the cDNAs was used to over-express recombinant protein with a C-terminal histidine tag Escherichia coli, which was affinity-purified. The antibody against the recombinant protein cross-reacted with proteins of 31–32 kDa in the membrane fraction from P. miliaceum mitochondria, but not with the chloroplast fraction. The recombinant protein reconstituted in liposomes efficiently transported malate, citrate, and 2-oxoglutarate.
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  • 8
    ISSN: 1617-4623
    Keywords: Phosphoenolpyruvate carboxylase ; DNA binding protein ; Zea mays ; C4 plant
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A plant nuclear protein PEP-I, which binds specifically to the promoter region of the phosphoenolpyruvate carboxylase (PEPC) gene, was identified. Methylation interference analysis and DNA binding assays using synthetic oligonucleotides revealed that PEP-I binds to GC-rich elements. These elements are directly repeated sequences in the promoter region of the PEPC gene and we have suggested that they may be cis-regulatory element of this gene. The consensus sequence of the element is CCCTCTCCACATCC and the CTCC is essential for binding of PEP-I. PEP-I is present in the nuclear extracts of green leaves, where the PEPC gene is expressed. However, no binding was detected in tissues where the PEPC gene is not expressed in vivo, such as roots or etiolated leaves. Thus, PEP-1 is the first factor identified in plants which has different binding activity in light-grown compared with dark-grown tissue. PEP-I binding is also tissue-specific, suggesting that PEP-1 may function to coordinate PEPC gene expression with respect to light and tissue specificity. This report describes the identification and characterization of the sequences required for PEP-1 binding.
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  • 9
    ISSN: 1573-5028
    Keywords: dicot ; mitochondria ; N-ethylmaleimide ; monocot ; phosphate transporter ; reconstitution
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract cDNA clones encoding mitochondrial phosphate transporters were isolated from four herbaceous plants. The cDNAs for the soybean, maize and rice transporters contained entire coding regions, whereas the Arabidopsis cDNA lacked the 5′ portion. The hydropathy profiles of the deduced amino acid sequences predicted the existence of six membrane-spanning domains which are highly conserved in the mitochondrial transporter family. In soybeans, the mRNA level for the transporter was high in tissues containing dividing cells. It was suggested that there are multiple copies of transporter genes in both dicots and monocots. The soybean transporter was expressed as inclusion bodies in Escherichia coli, solubilized with detergents, and then reconstituted into liposomes. The resulting proteoliposomes exhibited high phosphate transport activity. The activity was inhibited by N-ethylmaleimide, like those of mammalian phosphate transporters.
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  • 10
    ISSN: 1573-5028
    Keywords: cytokinin ; His-Asp phosphorelay ; histidine-containing phosphotransfer domain ; nitrogen signal transduction ; response regulator ; Zea mays
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Implication of His-to-Asp and/or Asp-to-His (His-Asp) phosphorelay has been recently reported in signal transduction pathways initiated by ethylene and cytokinin. These signaling systems are generally composed of sensor His-protein kinases, His-containing phosphotransfer (HPt) domains, and response regulator domains. In this study, we isolated maize cDNAs, designated as ZmRR2 and ZmHP2, which encode a response regulator domain and HPt domain, respectively, and we identified their His-to-Asp phosphotransfer activity in vitro. The putative translated product of ZmRR2 was highly similar to that of ZmRR1 (78% identity), a maize response regulator homologue. The putative translated product of ZmHP2 showed similarity to that of HPt domains from Arabidopsis thaliana (AHP1–AHP3: 44 to 47% identity) and Saccharomyces cerevisiae (Ypd1p: 24% identity). In vitro experiments demonstrated that the putative signaling factors can transfer the phosphoryl group from His-80 of ZmHP2 to Asp-90 of ZmRRs. Treating detached leaves with t-zeatin or supplying inorganic nitrogen to the whole plant induced the accumulation of ZmRR1 and ZmRR2 transcripts. On the other hand, the steady-state transcript level of ZmHP2 was not affected by cytokinin or inorganic nitrogen sources. These results indicate that His-Asp phosphotransfer may be involved in the transduction of nitrogen signals mediated by cytokinin, and that multiple response regulators participate in the signaling pathways.
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