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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of agricultural and food chemistry 35 (1987), S. 122-126 
    ISSN: 1520-5118
    Source: ACS Legacy Archives
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 24 (1968), S. 941-943 
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Résumé Chez les cailles japonaises, le complexe glandulaire du cloaque est en fait localisé dans la lèvre dorsale du cloaque et non de l'anus. Il existe un complexe glandulaire similaire et très petit du côté ventral. La glande active se colore intensément avec le réactif périodique «acide Schiff», avec la fuchsine aldéhyde, avec le bleu d'alciane et métachromatiquement avec le bleu de toluidine. Ceci indique la présence d'une sécrétion de glycomucoprotéines. Le liquide transparent sécrété est transformé en masse blanche mousseuse au contact des bactériesE. coli etProteus mirabilis, présentes en quantités équivalentes dans le proctodeum. Les gaz émis consistent probablement en H2 et CO2, ce dernier peut agir comme tampon et stabiliser le pH de la sécrétion autour de la valeur 6,5.
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  • 3
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 269 (1977), S. 406-407 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Nitrate reductase-deficient mutants were induced with sodium azide in 'Steptoe' barley (Hordeum vulgare L.) as described by Kleinhofs et al.7'*. Steptoe barley seeds were hydrated at 0-2 C overnight and then germinated at 20 C in vigorously aerated water for 8 h. The seeds were then placed in ...
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Theoretical and applied genetics 85 (1992), S. 274-275 
    ISSN: 1432-2242
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Theoretical and applied genetics 74 (1987), S. 714-717 
    ISSN: 1432-2242
    Keywords: Hordeum vulgare ; Mutants ; Nitrate reductase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary NADH-specific and NAD(P)H bispecific nitrate reductases are present in barley (Hordeum vulgare L.). Wild-type leaves have only the NADH-specific enzyme while mutants with defects in the NADH nitrate reductase structural gene (nar1) have the NAD(P)H bispecific enzyme. A mutant deficient in the NAD(P)H nitrate reductase was isolated in a line (nar1a) deficient in the NADH nitrate reductase structural gene. The double mutant (nar1a;nar7w) lacks NAD(P)H nitrate reductase activity and has xanthine dehydrogenase and nitrite reductase activities similar to nar1a. NAD(P)H nitrate reductase activity in this mutant is controlled by a single codominant gene designated nar7. The nar7 locus appears to be the NAD(P)H nitrate reductase structural gene and is not closely linked to nar1. From segregating progeny of a cross between the wild type and nar1a;nar7w, a line was obtained which has the same NADH nitrate reductase activity as the wild type in both the roots and leaves but lacks NADPH nitrate reductase activity in the roots. This line is assumed to have the genotype Nar1Nar1nar7nar7. Roots of wild type seedlings have both nitrate reductases as shown by differential inactivation of the NADH and NAD(P)H nitrate reductases by a monospecific NADH-nitrate reductase antiserum. Thus, nar7 controls the NAD(P)H nitrate reductase in roots and in leaves of barley.
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Theoretical and applied genetics 75 (1988), S. 767-771 
    ISSN: 1432-2242
    Keywords: Hordeum vulgare ; Nitrate reductase ; Linkage ; Mutants
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The nar2 locus that codes for a protein involved in molybdenum cofactor function in nitrate reductase and other molybdoenzymes was mapped to barley chromosome 7. F2 genotypic data from F3 head rows indicated nar2 is located 8.4±2.1 and 23.0± 4.6 cm from the narrow leaf dwarf (nld) and mottled seedling (mt2) loci, respectively. This locates the nar2 locus at 54.7±3.1 cm from the short-haired rachilla (s) locus near the centromere of chromosome 7. Close linkage of nar2 with DDT resistance (ddt) and high lysine (lys3) loci was detected but could not be quantified due to deviations from the individual expected 1∶2∶1 segregations for the ddt and lys3 genes. Southern blots of wheat-barley addition lines probed with a nitrate reductase cDNA located the NADH : nitrate reductase structural gene, nar1, to chromosome 6.
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Theoretical and applied genetics 88 (1994), S. 589-592 
    ISSN: 1432-2242
    Keywords: Hordeum ; Triticum ; Grasses ; Gene deletion ; Gene duplication
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Cultivated barley,Hordeum vulgare L., has a single NADH nitrate reductase (NR) gene while diploid wheat,Triticum monococcum, and cultivated hexaploid wheat,Triticum aestivum L., have two NADH NR genes. To determine whether the NADH NR gene was duplicated since the divergence ofTriticum fromHordeum or was deleted from barley, theT. Monococcum NADH NR gene heme-hinge regions were sequenced and compared with the barley NADH NR gene sequence. Sequence identity and phylogenetic analyses showed that one of theT. Monococcum NADH NR genes is more-closely related to the barley NADH NR gene than to the otherT. Monococcum NADH NR gene. The heme-hinge region of all three NR genes appeared to have evolved at a constant rate. These results suggest that the NADH NR gene duplicated before the divergence ofTriticum andHordeum and that a deletion resulted in the loss of one NADH NR gene from cultivated barley.
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  • 8
    ISSN: 1573-4927
    Keywords: Pisum sativum ; nitrate reductase ; mutants ; molybdenum cofactor disturbed
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Two nitrate reductase (NaR)-deficient mutants of pea (Pisum sativum L.), E1 and A300, both disturbed in the molybdenum cofactor function and isolated, respectively, from cv Rondo and cv Juneau, were tested for allelism and were compared in biochemical and growth characteristics. The F1 plants of the cross E1 × A300 possessed NaR and xanthine dehydrogenase (XDH) activities comparable to those of the wild types, indicating that these mutants belong to different complementation groups, representing two different loci. Therefore, mutant E1 represents, besides mutant A300 and the allelic mutants A317 and A334, a third locus governing NaR and is assigned the gene destignation nar 3. In comparison with the wild types, cytochrome c reductase activity was increased in both mutants. The mutants had different cytochrome c reductase distribution patterns, indicating that mutant A300 could be disturbed in the ability to dimerize NaR apoprotein monomers, and mutant E1 in the catalytic function of the molybdenum cofactor. In growth characteristics studied, A300 did not differ from the wild types, whereas fully grown leaves of mutant E1 became necrotic in soil and in liquid media containing nitrate.
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    Molecular genetics and genomics 181 (1981), S. 20-23 
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Ten nitrate reductase (NR)-deficient mutants have been characterized for their cross-reactivity against specific barley (Hordeum vulgare L.) nitrate reductase antibodies. The rabbit antibodies raised against the purified barley wild type (cv. Steptoe) enzyme quantitatively inactivate nitrate reductase in crude extracts. All nitrate-grown (induced) mutants show positive precipitin reaction against the antiserum by Ouchterlony double diffusion test and all have the ability to neutralize antisera in a NR protection assay. Under induced growth conditions, mutants Az 12, Az 23, Az 29 and Az 30 which have low NR associated catalytic activities also have the lowest level of antigenicity; mutants Az 13, Az 31, Az 33 and Az 34 have intermediate level of both NR associated catalytic activities and antigenicity, while mutants Az 28 and Az 32 have the highest level of both NR associated catalytic activities and antigenicity. Under noninduced growth conditions, all mutants except Az 12 contain detectable but very low levels of NR antigenicity. These results support the concept that these NR-deficient mutants with various levels of NR associated catalytic activities represent different mutation events at the loci coding the NR structural components.
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    Molecular genetics and genomics 177 (1980), S. 421-425 
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Ten nitrate reductase-deficient Hordeum vulgare mutants were characterized for NADH and FMNH2 nitrate reductase (NR), cytochrome C reductase (CR) and nitrite reductase (NiR) activities. The mutants sort into four major groups. Group I represented by mutants Az 12, Az 23, Az 29 and Az 30 have low Nr and Cr activities. Group II represented by mutants Az 13, Az 31, Az 33 and Az 34 have low NR activities but intermediate CR activities. Group III represented by mutant Az 28 has low NR activity, but above normal CR activity. Group IV represented by Az 32 has low NADH-NR, low CR, but above normal FMNH2-NR activity. All ten mutants have elevated NiR activities. None of the ten mutants were constitutive for nitrite reductase activity. Only Az 34 showed a definite high temperature sensitivity when the NADH nitrate reductase activity was compared in the 12 to 26° C range. The mutants Az 12, Az 13, Az 23, Az 28, Az 29, Az 30, Az 31, Az 32 and Az 33 are allelic and were assigned the locus designation nar1. Mutant Az 34 represents a different genetic locus designated nar2. The nar1 gene is codominant and the nar2 gene is recessive.
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