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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
    Isolation and characterization of a cDNA encoding NADP+-specific isocitrate dehydrogenase from soybean (Glycine max) (1993)
    Springer
    Plant molecular biology 21 (1993), S. 739-752 
    Details
    ISSN: 1573-5028
    Keywords: cDNA ; isocitrate dehydrogenase ; DNA sequence ; soybean ; mRNA
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A cDNA that encodes an NADP-specific isocitrate dehydrogenase (IDH) was cloned from a soybean nodule cDNA library by complementation of an Escherichia coli mutant that lacked IDH. DNA sequence analysis showed that the 1583 bp soybean cDNA could encode a protein that shares 63.9% amino acid sequence identity with the Saccharomyces cerevisiae NADP-IDH and long sequences of identity to an IDH from pig. Southern blot analysis suggests that this gene corresponds to a gene family made up of no more than two loci. The IDH cDNA hybridized to a 1.7 kb soybean mRNA and the relative amount of this transcript in soybean leaves, nodules and roots was 1:3.4:7.7. In alfalfa, a 1.7 kb mRNA was also found but the ratios for the corresponding tissues were 1:7.4:7.7. IDH activity was detected in the complemented E. coli strain and the electrophoretic mobility of this activity in nondenaturing polyacrylamide gels was identical to that of an IDH in extracts from soybean cotyledons or nodule cytosol. NADP-IDH specific activity in the E. coli host strain varied with growth phase; the highest rates (ca. 180 nmol/min per mg protein) were observed in late-stationary-phase cells. The enzyme had a broad pH optimum of 8.0 to 9.5 and had an absolute metal cofactor requirement, preferring Mn2+ below pH 8.0 and Mg2+ above pH 8.0. The K m for isocitrate and NADP was 21 μM and 11 μM respectively with Mn2+ as cofactor and 13 μM and 12 μM with Mg2+ as cofactor.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00027108
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  • 4
    Electronic Resource
    Electronic Resource
    Characterization of two proteinase inhibitor (ATI) cDNAs from alfalfa leaves (Medicago sativa var. Vernema): the expression of ATI genes in response to wounding and soil microorganisms (1995)
    Springer
    Plant molecular biology 27 (1995), S. 995-1001 
    Details
    ISSN: 1573-5028
    Keywords: alfalfa ; Bowman-Birk ; proteinase inhibitors ; soil microorganisms ; wounding
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract cDNAs encoding two Bowman-Birk proteinase inhibitors were isolated from the leaves of alfalfa (Medicago sativa). The cDNAs are derived from a small gene family (3 to 10 genes) encoding alfalfa trypsin inhibitors (ATIs). Each cDNA clone encoded a mature ATI that was part of a larger, putative preprotein. ATI mRNAs are continuously expressed in flower parts, but are mechanically wound-inducible in the stems and leaves. ATI mRNA is shown to be continuously present in roots of soil-grown plants, but its presence is primarily in response to microorganisms present in the soil. Additionally, while mechanical wounding of the alfalfa roots induced ATI mRNA synthesis both in the roots and in the leaves, microbial infection of the roots triggered ATI mRNA synthesis in the roots but not in the leaves. These results suggest that both local and systemic signalling pathways for proteinase inhibitor synthesis are present in alfalfa plants.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00037026
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  • 5
    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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  • 6
    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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  • 7
    Electronic Resource
    Electronic Resource
    Genetic analysis of bacteriophage P4 using P4-plasmid ColE1 hybrids (1980)
    Springer
    Molecular genetics and genomics 177 (1980), S. 399-412 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A set of plasmids that contain fragments of the bacteriophage P4 genome has been constructed by deleting portions of a P4-ColE1 hybrid. A P4 genetic map has been established and related to the physical map by examining the ability of these plasmids to rescue various P4 mutations. The P4 vir1 mutation and P4 genes involved in DNA replication (α), activation of P2 helper genes (δ and ε), polarity suppression (psu) and head size determination (sid) have been mapped, as has the region responsible for synthesis of a nonessential P4 protein. One of the deleted plasmids contains only 5900 base pairs (52%) of P4 but will form plaques if additional DNA is added to increase its total size to near that of P4. This plasmid is also unique in that it will not form stable associations with P2 lysogens of E. coli which are recA +. P4 α mutants can be suppressed as a result of replication under control of the ColE1 part of the hybrid.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00271478
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  • 8
    Electronic Resource
    Electronic Resource
    Cloning of the integration and attachment regions of bacteriophage P4 (1984)
    Springer
    Molecular genetics and genomics 195 (1984), S. 44-51 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The integration and attachment regions of bacteriophage P4 have been cloned into a multicopy plasmid. This plasmid can integrate into the E. coli chromosome at the same location as the parent phage. Integration increases the stability of the plasmid and allows it to be retained even under conditions in which a non-integrated plasmid would be lost. None of the genes needed for P4 lytic growth is required for integration. The P4 integration and attachment regions have been cloned on separate plasmids. A plasmid that carries the attachment site can integrate into the chromosome only if another plasmid that carries the P4 integration functions is present. A plasmid that carries only this trans-acting integration function cannot integrate. Using deletion mutants of the plasmid, the maximum size of the region needed for integration has been determined to be 1.6 kb, of which no more than 1.2 kb codes for the integrase protein. A nonsense mutant defective in integration has been isolated by using a rapid screening procedure that identifies unstable plasmids.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00332722
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  • 9
    Electronic Resource
    Electronic Resource
    Distribution of two isoforms of NADP-dependent isocitrate dehydrogenase in soybean (Glycine max) (1999)
    Springer
    Plant molecular biology 40 (1999), S. 13-21 
    Details
    ISSN: 1573-5028
    Keywords: carbon metabolism ; isocitrate dehydrogenase ; isozymes ; nitrogen fixation ; soybean ; TCA cycle
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Two different cDNAs that encode NADP-specific isocitrate dehydrogenase (NADP-IDH) isozymes of soybean (Glycine max) were characterized. The nucleotide sequences of the coding regions of these cDNAs have 74% identity to each other and give predicted amino acid sequences that have 83% identity to each other. Using PCR techniques, their coding regions were subcloned into a protein overexpression vector, pQE32, to yield pIDH4 and pIDH1, respectively. Both IDH4 and IDH1 enzymes were expressed in Escherichia coli as catalytically active His6 tagged proteins, purified to homogeneity by affinity chromatography on nickel chelate resin and rabbit polyclonal antibodies to each were generated. Surprisingly, antiserum to IDH4 did not react with IDH1 protein and IDH1 antiserum reacted only very weakly with IDH4 protein. IDH4 antibody reacts with a protein of expected molecular weight in cotyledon, young leaf, young root, mature root and nodules but the reaction with mature leaf tissue was low compared to other tissues. Western blot results show that IDH1 was not expressed in young roots but a protein that reacts with the IDH1 antibody was highly expressed in leaves, showing that there was tissue-specific accumulation of NADP-IDH isozymes in soybean.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1026464704134
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  • 10
    Electronic Resource
    Electronic Resource
    Phosphorus uptake by bean nodules (1998)
    Springer
    Plant and soil 198 (1998), S. 71-78 
    Details
    ISSN: 1573-5036
    Keywords: legumes ; Phaseolus vulgaris ; phosphorus metabolism ; Rhizobium tropici
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract Phosphate (P) uptake experiments were conducted to determine the routes of P entry into nitrogen-fixing common bean root nodules and the availability of this P to the bacteroids within the nodules. Nodulated common bean plants were cultured for 30 days in a hydroponic system that contained either a complete nutrient solution (+P) or a nutrient solution where P was not added (−P). The plant roots were then exposed to [32P]-phosphate-labeled +P nutrient solution and P accumulation in bacteroids and nodules was measured. For labeling, plants were suspended in the nutrient solution so that the root system was either fully or partially submerged. Because bean nodules are heavily clustered in the root crown, most of the nodules in the partial submergence treatments were not in contact with the nutrient solution and we could study nodules that had not been directly exposed to 32P. Regardless of P treatment of the host plant, P accumulation in bacteroids was significantly greater and more rapid when the nodule surface was in contact with the labeled nutrient solution, suggesting that nodules can import P from the solution. P entry through the nodule surface was verified in experiments where 32P-labeled nutrient solution was applied to the nodule surface only. In full submergence treatments, 32P accumulation in bacteroids of −P plants was significantly greater than in bacteroids of +P plants. As measured by total leaf label, uptake and translocation of P to the shoot was greater in −P plants and still greater in partial submergence treatments where most of the nodules were not in contact with the labeled nutrient solution. Results of these experiments suggest that, in addition to P acquisition via the vascular system, P flow to symbiotic tissues and bacteroids can originate from the soil solution immediately surrounding the nodule. This was particularly evident in nodules of plants that had been limited for P.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1004200903458
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