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  • 81.15  (1)
  • Abscisic acid  (1)
  • 1
    ISSN: 1432-0630
    Schlagwort(e): 81.15 ; 68.55 ; 07.80
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Maschinenbau , Physik
    Notizen: Abstract Thin films of pure copper have been deposited on glass and Si(100) substrates using copper acetylacetonate [Cu(acac)2] and copper HexaFluoroAcetylacetonate [Cu(HFA)2] sources. A thermal, cold-wall, reduced pressure (3325–5985 Pa) Metal-Organic Chemical Vapor Deposition (MOCVD) process was employed. The effect of H2O vapor on the grain size, deposition rate, and resistivity was examined. Electrical resistivities of 2.4 μω cm for copper films deposited on Si(100) and 3.44 μω cm for copper films deposited on glass at substrate temperatures of 265° C and a [Cu(acac)2] source temperature of 147° C with the use of H2O vapor were measured. When [Cu(HFA)2] was used, the substrate temperature was 385° C and the source temperature was 85° C. An activation energy for the copper film deposition process was calculated to be 22.2 kJ/mol in the case of the [Cu(acac)2] source. A deposition rate of 11 nm/min was obtained with Cu(acac)2 as the source and the rate was 44.4 nm/min with the Cu(HFA)2 source; both were obtained with the use of H2O vapor. No selectivity was observed with either source for either substrate. The deposited films were fully characterized using XRD, LVSEM, SAXPS, and RBS.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    ISSN: 1617-4623
    Schlagwort(e): Key words Protein phosphorylation ; Osmotic stress Serine protein kinase ; Abscisic acid
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract Two soybean cDNA clones, SPK-3 and SPK-4, encoding putative protein kinases were isolated and characterized. Both cDNAs encoded approximately 40-kDa serine/threonine kinases with unusual stretches of acidic amino acids in their carboxy-terminal regions, which are highly homologous to PKABA1 from wheat and ASKs from Arabidopsis. These kinases are encoded by one- or two-copy genes in the soybean genome. Notably, SPK-3 and -4 showed different patterns of expression in various soybean tissues. SPK-3 is highly expressed in dividing and elongating tissues of young seedlings but relatively weakly in tissues of mature plants. In contrast, SPK-4 showed relatively high and constitutive expression in all the tissues examined except for leaf tissues of mature plants. Although various stressors, such as dehydration and high salinity, increased the expression of both genes, the induction kinetics were different. The two genes also differed in their response to abscisic acid (ABA). SPK-3 was induced but SPK-4 was not affected by exogenously supplied abscisic acid. In accordance with these expression data analysis of the activity of a chimeric SPK-3 promoter::β-glucuronidase (GUS) reporter gene by transient expression in tobacco leaves confirmed the inducibility of SPK-3 by salt and ABA. Polyclonal antibodies raised against a recombinant SPK-4 protein produced in Escherichia coli specifically recognized both recombinant SPK-3 and -4 proteins. Kinase assays using affinity-purified SPK-4/antibody complexes with crude soybean extracts as substrate identified specific phosphorylation of two 41 and 170 kDa soybean proteins that were phosphorylated on serine residues. Taken together, our results suggest that SPK-3, and/or SPK-4 are functional serine protein kinase(s). Furthermore, SPK-3 and -4 may play different roles in the transduction of various environmental stresses.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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