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  • 1
    Electronic Resource
    Electronic Resource
    Human awakening and subsequent identification of fire-related cues (1984)
    Springer
    Fire technology 20 (1984), S. 20-26 
    Details
    ISSN: 1572-8099
    Keywords: Fire-related cues ; cue effectiveness ; cue detection ; response time ; human awakening ; human detection ; alarm attenuation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Architecture, Civil Engineering, Surveying
    Notes: Abstract Twenty-four college-age male subjects, employed for one night each, were evaluated on their ability to awaken and then identify fire cues. Twelve subjects were exposed to smoke alarm warning signals of three intensities, while the second twelve subjects were exposed to a smoke odor, a heat presentation, and a single smoke alarm warning signal. Subjects were, in all cases, awakened by alarms that reached their ears at signal/noise ratios of 34 dB. They were considerably less likely to be awakened by heat, the smoke odor, and alarm sounds that reached their ears at signal/noise ratios of 10 dB or less. Upon awakening, subjects repeatedly failed to correctly label radiant heat presentations and smoke alarm warnings as fire cues.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02390045
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  • 2
    Electronic Resource
    Electronic Resource
    Cellular localization of nodule-enhanced aspartate aminotransferase inMedicago sativa L. (1994)
    Springer
    Planta 192 (1994), S. 202-210 
    Details
    ISSN: 1432-2048
    Keywords: Aspartate aminotransferase (immunocytochemistry, subcellular fractionation) ; Glutamate oxaloacetic transaminase ; Medicago (root nodules, N2 fixation) ; Nitrogen fixation ; Root nodule
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Aspartate aminotransferase (AAT; EC 2.6.1.1) catalyzes the synthesis of the amino acid aspartate which, in alfalfa root nodules, serves as the immediate precursor of the primary N-transport compound, asparagine. The enzyme AAT may also be important in providing substrates for host-plant and bacteroid respiration. The enzyme occurs as two isoenzymes, AAT-1 and AAT-2, with AAT-1 more abundant in roots and AAT-2 predominant in root nodules. To further elucidate the role of AAT in root-nodule metabolism, subcellular fractionation and immunocytochemical methods were used to determine the intra- and intercellular localization of these two isozymes. Fractionation of nodule subcellular components showed that AAT-2 was localized in amyloplasts. Immunogold labelling with AAT-2 antibodies unequivocally confirmed this, showing that AAT-2 was localized in nodule amyloplasts and leaf chloroplasts. In root nodules, the density of immunogold labelling of infected cell plastids was almost four times that of uninfected cell plastids. The data suggest that aspartate biosynthesis in alfalfa root nodules occurs primarily in the plastids of infected cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01089036
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  • 3
    Electronic Resource
    Electronic Resource
    Cellular localization of nodule-enhanced aspartate aminotransferase in Medicago sativa L. (1994)
    Springer
    Planta 192 (1994), S. 202-210 
    Details
    ISSN: 1432-2048
    Keywords: Aspartate aminotransferase (immunocytochemistry, subcellular fractionation) ; Glutamate oxaloacetic transaminase ; Medicago (root nodules, N2 fixation) ; Nitrogen fixation ; Root nodule
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Aspartate aminotransferase (AAT; EC 2.6.1.1) catalyzes the synthesis of the amino acid aspartate which, in alfalfa root nodules, serves as the immediate precursor of the primary N-transport compound, asparagine. The enzyme AAT may also be important in providing substrates for host-plant and bacteroid respiration. The enzyme occurs as two isoenzymes, AAT-1 and AAT-2, with AAT-1 more abundant in roots and AAT-2 predominant in root nodules. To further elucidate the role of AAT in root-nodule metabolism, subcellular fractionation and immunocytochemical methods were used to determine the intra- and intercellular localization of these two isozymes. Fractionation of nodule subcellular components showed that AAT-2 was localized in amyloplasts. Immunogold labelling with AAT-2 antibodies unequivocally confirmed this, showing that AAT-2 was localized in nodule amyloplasts and leaf chloroplasts. In root nodules, the density of immunogold labelling of infected cell plastids was almost four times that of uninfected cell plastids. The data suggest that aspartate biosynthesis in alfalfa root nodules occurs primarily in the plastids of infected cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00194454
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  • 4
    Electronic Resource
    Electronic Resource
    Isolation and analysis of a cDNA clone that encodes an alfalfa (Medicago sativa) aspartate aminotransferase (1991)
    Springer
    Molecular genetics and genomics 231 (1991), S. 97-105 
    Details
    ISSN: 1617-4623
    Keywords: Aspartate aminotransferase ; Alfalfa ; Nitrogen fixation ; Symbiosis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary We have isolated an alfalfa leaf cDNA clone that encodes aspartate aminotransferase (AAT, EC 2.6.1.1) by direct complementation of an Escherichia coli aspartate auxotroph with a plasmid cDNA library. DNA sequence analysis of the recombinant plasmid, pMU1, revealed that a 1514 by cDNA was inserted in the correct orientation and in-frame with the start of the lacZ coding sequence in the vector, pUC18. The resulting fusion protein is predicted to be 424 amino acids in length with a molecular weight of 46387 Daltons. The cDNA-encoded protein has a characteristic pyridoxal phosphate attachment site motif and has substantial amino acid sequence homology to both animal and bacterial AATs. Plasmid pMUl encodes an AAT with a Km for aspartate of 3.3 mM, a Km for 2-oxoglutarate of 0.28 mM, and a pH optimum between 8.0 and 8.5. Several lines of evidence including Western blot analysis, the isoelectric point of the encoded protein, and the effect of pH on the activity of the fusion protein, suggest that the cDNA encodes the isozyme AAT-1 rather than AAT-2. Northern blot analysis showed that the aat-1 clone hybridized to a 1.6 kb transcript present in alfalfa leaves, roots and nodules. The relative concentrations of aat-1 mRNA in these tissues were 1: 2: 5, respectively. Thus, transcription of aat-1 appears to be induced during nodule development. Southern blot analysis suggested that AAT-1 in alfalfa is encoded by either a single-copy gene or a small, multigene family.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00293827
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