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  • 1
    Electronic Resource
    Electronic Resource
    Measurement of the static error rate of a storage cell for single magnetic flux quanta, fabricated from high-Tc multilayer bicrystal Josephson junctions (1998)
    Woodbury, NY : American Institute of Physics (AIP)
    Applied Physics Letters 72 (1998), S. 1513-1515 
    Details
    ISSN: 1077-3118
    Source: AIP Digital Archive
    Topics: Physics
    Notes: We measured the static error rate of a high-Tc superconductor dc superconducting quantum interference device (SQUID), which, in the form as a storage loop for single flux quanta, is a basic element of rapid single flux quantum circuits. Using high-Tc multilayer bicrystal technology, we fabricated a stacked dc SQUID pair, one SQUID serving as the storage loop, the other one as the readout device. The escape rate of a stored flux quantum was measured as a function of the bias current at a temperature of 28 K. The measured error rates were in good agreement with a model calculation based on thermally activated barrier crossing. © 1998 American Institute of Physics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.121043
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  • 2
    Electronic Resource
    Electronic Resource
    Resonant tunneling transport across YBa2Cu3O7–SrRuO3 interfaces (1995)
    Woodbury, NY : American Institute of Physics (AIP)
    Applied Physics Letters 67 (1995), S. 1775-1777 
    Details
    ISSN: 1077-3118
    Source: AIP Digital Archive
    Topics: Physics
    Notes: We have investigated superconductor–normal metal–superconductor junctions with metallic perovskite SrRuO3 barriers. Ramp-type junctions with ion-beam-etched and wet-chemical-etched YBa2Cu3O7 (YBCO) ramps have been compared with planar junctions where the interfaces were fabricated completely in situ. Regardless of the fabrication method, the junction properties were determined not by the metallic SrRuO3 barrier, but by an insulating layer at the interface. The shape of the I–V curves, and the temperature dependence of the normal resistance of junctions, could be well explained by quasiparticle resonant tunneling via two localized states in the interface layer. Furthermore, a model for the Cooper pair transport will be discussed that assumes resonant tunneling via one localized state as transport mechanism. © 1995 American Institute of Physics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.114379
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  • 3
    Electronic Resource
    Electronic Resource
    Circulardichroismus-XIX - Nitrosamine und nitrosaminoketale. Sektorregel fur nitrosamine, nitroverbindungen und lactone
    Amsterdam : Elsevier
    Tetrahedron 22 (1966), S. 3103-3116 
    Details
    ISSN: 0040-4020
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/S0040-4020(01)82289-4
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  • 4
    Electronic Resource
    Electronic Resource
    Multiple scattering of plasmons at rough surfaces
    Amsterdam : Elsevier
    Optics Communications 21 (1977), S. 173-176 
    Details
    ISSN: 0030-4018
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0030-4018(77)90103-1
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  • 5
    Electronic Resource
    Electronic Resource
    Specific subunit pairs of legumin from Vicia faba
    Amsterdam : Elsevier
    Phytochemistry 22 (1983), S. 1861-1866 
    Details
    ISSN: 0031-9422
    Keywords: Leguminosae ; Vicia faba ; field bean ; legumin ; subunit heterogeneity.
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0031-9422(83)80002-8
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  • 6
    Electronic Resource
    Electronic Resource
    Cloning and expression of an Arxula adeninivorans glucoamylase gene in Saccharomyces cerevisiae (1996)
    Springer
    Applied microbiology and biotechnology 44 (1996), S. 610-619 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract The glucoamylase gene of the yeast Arxula adeninivorans Ls3 has been cloned from a genomic library and sequenced. The gene could be localized on chromosome 2 from A. adeninivorans and comprises 1875 bp. The first 16 N-terminal amino acids represent the signal sequence for entering the endomembrane system. Comparing the amino acid sequence from this glucoamylase with those of other fungal glucoamylases shows that the glucoamylase of strain Ls3 has a homology to the glucoamylases from Rhizopus oryzae (32.6%), Saccharomycopsis fibuligera (23.1%), Aspergillus niger (22.1%), and Saccharomyces diastaticus (15.4%). No homology could be detected to the glucoamylase of Schwanniomyces occidentalis. By using the GAL1 promoter from Saccharomyces cerevisiae within an autonomously replicating plasmid it was possible to express the isolated Arxula glucoamylase gene in Saccharomyces cerevisiae. The transformants secreted 95% of the enzyme into the culture medium. The N termini of glucoamylases synthesized in A. adeninivorans and S. cerevisiae transformants are identical, which means that the signal sequences were cleaved at the same positions during maturation of the proteins. The highest glucoamylase activities were reached in the culture medium of S. cerevisiae transformants after 36 h of fermentation. Northern hybridization showed that the glucoamylase transcripts were formed continuously for up to 70 h. These results reveal that the glucoamylase is expressed and secreted more rapidly in the S. cerevisiae transformants than in A. adeninivorans Ls3.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00172493
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  • 7
    Electronic Resource
    Electronic Resource
    Cloning and expression of an Arxula adeninivorans glucoamylase gene in Saccharomyces cerevisiae (1996)
    Springer
    Applied microbiology and biotechnology 44 (1996), S. 610-619 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  The glucoamylase gene of the yeast Arxula adeninivorans Ls3 has been cloned from a genomic library and sequenced. The gene could be localized on chromosome 2 from A. adeninivorans and comprises 1875 bp. The first 16 N-terminal amino acids represent the signal sequence for entering the endomembrane system. Comparing the amino acid sequence from this glucoamylase with those of other fungal glucoamylases shows that the glucoamylase of strain Ls3 has a homology to the glucoamylases from Rhizopus oryzae (32.6%), Saccharomycopsis fibuligera (23.1%), Aspergillus niger (22.1%), and Saccharomyces diastaticus (15.4%). No homology could be detected to the glucoamylase of Schwanniomyces occidentalis. By using the GAL1 promoter from Saccharomyces cerevisiae within an autonomously replicating plasmid it was possible to express the isolated Arxula glucoamylase gene in Saccharomyces cerevisiae. The transformants secreted 95% of the enzyme into the culture medium. The N termini of glucoamylases synthesized in A. adeninivorans and S. cerevisiae transformants are identical, which means that the signal sequences were cleaved at the same positions during maturation of the proteins. The highest glucoamylase activities were reached in the culture medium of S. cerevisiae transformants after 36 h of fermentation. Northern hybridization showed that the glucoamylase transcripts were formed continuously for up to 70 h. These results reveal that the glucoamylase is expressed and secreted more rapidly in the S. cerevisiae transformants than in A. adeninivorans Ls3.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002530050607
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  • 8
    Electronic Resource
    Electronic Resource
    Expression of the Arxula adeninivorans glucoamylase gene in Kluyveromyces lactis (1996)
    Springer
    Applied microbiology and biotechnology 45 (1996), S. 102-106 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  The glucoamylase gene of the yeast Arxula adeninivorans was expressed in Kluyveromyces lactis by using the GAP promoter from Saccharomyces cerevisiae and a multicopy plasmid vector. The transformants secreted 90.1% of the synthesized glucoamylase into the culture medium. The secreted glucoamylase activities are about 20 times higher in comparison to those of Saccharomyces cerevisiae transformants using the same promoter. Secreted glucoamylase possesses identical N-terminal amino acid sequences to those secreted by A. adeninivorans showing that cleavage of the N-terminal signal peptide takes place at the same site. Biochemical characteristics of glucoamylase expressed by K. lactis and A. adeninivorans are very similar.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002530050655
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  • 9
    Electronic Resource
    Electronic Resource
    Polymorphism of legumin subunits from field bean (Vicia faba L. var. minor) and its relation to the corresponding multigene family (1993)
    Springer
    Theoretical and applied genetics 86 (1993), S. 867-874 
    Details
    ISSN: 1432-2242
    Keywords: cDNA ; Legumin subunits ; Polymorphism ; Gene assignment ; Vicia faba
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Legumin, which amounts to approximately 55% of the seed protein in field beans (Vicia faba L. var. minor), is a representative of the 12S storage globulin family. The 12S storage globulins are hexameric holoprotein molecules composed of different types of polymorphic subunits encoded by a multigene family. ‘Type-A’ legumin subunits contain methionine whereas ‘type-B’ are methionine-free subunits. Sequencing of two different type A-specific cDNAs, as well as an FPLC/HPLC-based improvement of subunit fractionation and peptide mapping with subsequent partial amino-acid sequencing, permit the assignment of some of the polymorphic legumin subunits to members of the multigene family. Two different type A subunits (A1 and A2) correspond to the two different cDNA clones pVfLa129 (A2) and 165 (A1), but microheterogeneity in the amino-acid sequences indicates that polymorphic variants of both representatives of this type may exist. Two groups of published type B-specific gene sequences (LeB7, and LeB2, LeB4, LeB6, respectively) are represented by two polymorphic subunit fractions (B3I, B3II, and B4I, B4II). A seventh clone, LeB3, encodes one of the large legumin subunits that is only a minor component of the legumin seed protein complex.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00212614
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  • 10
    Electronic Resource
    Electronic Resource
    The families of papain- and legumain-like cysteine proteinases from embryonic axes and cotyledons of Vicia seeds: developmental patterns, intracellular localization and functions in globulin proteolysis (2000)
    Springer
    Plant molecular biology 43 (2000), S. 83-101 
    Details
    ISSN: 1573-5028
    Keywords: cysteine proteinases ; differential gene expression ; enzyme families ; seed globulin proteolysis ; vacuolar localization ; Vicia sativa
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Families of papain- and legumain-like cysteine proteinases (CPR) were found in Vicia seeds. cDNAs and antibodies were used to follow organ specificity and the developmental course of CPR-specific mRNAs and polypeptides. Four papain-like cysteine proteinases (CPR1, CPR2, proteinase A and CPR4) from vetch seeds (Vicia sativa L.) were analysed. CPR2 and its mRNA were already found in dry embryonic axes. CPR1 was only detected there during early germination. Both CPR1 and CPR2 strongly increased later during germination. In cotyledons, both CPR1 and CPR2 were only observed one to two days later than in the axis. Proteinase A was not found in axes. In cotyledons it could only be detected several days after seeds had germinated. CPR4 mRNA and polypeptide were already present in embryonic axes and cotyledons during seed maturation and decreased in both organs during germination. Purified CPR1, CPR2 and proteinase A exhibited partially different patterns of globulin degradation products in vitro. Although the cDNA-deduced amino acid sequence of the precursor of proteinase A has an N-terminal signal peptide, the enzyme was not found in vacuoles whereas the other papain-like CPRs showed vacuolar localization. Four different legumain-like cysteine proteinases (VsPB2, proteinase B, VnPB1 and VnPB2) of Vicia species were analysed. Proteinase B and VnPB1 mRNAs were detected in cotyledons and seedling organs after seeds had germinated. Proteinase B degraded globulins isolated from mature vetch seeds in vitro. VsPB2 and proteinase B are localized to protein bodies of maturing seeds and seedlings, respectively, of V. sativa. Like VsPB2 from V. sativa, also VnPB2 of V. narbonensis corresponds to vacuolar processing enzymes (βVPE). Based on these results different functions in molecular maturation and mobilization of storage proteins could be attributed to the various members of the CPR families.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006456615373
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