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  • 1990-1994  (4)
  • 1980-1984  (4)
  • 1920-1924
  • 1900-1904
  • 1990  (4)
  • 1980  (4)
Material
Years
  • 1990-1994  (4)
  • 1980-1984  (4)
  • 1920-1924
  • 1900-1904
Year
  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 4 (1990), S. 0 
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The three nodD genes of a strain of Rhizobium leguminosarum biovar phaseoli were cloned to study their effects on transcription of themselves and of the nodC genes of biovars phaseoli and viciae. Efficient transcription of nodD1 required nodD1 and was enhanced by exposure of the cells to bean exudate consistent with the presence of a nod-box preceding the nolE-nodD1 operon. Transcription of nodD2 and nodDZ was constitutive. nodC of R. leguminosarum biovar phaseoli was activated by each of the nodD genes of that biovar in the absence of inducers but expression was enhanced in cells grown with bean exudate or the flavonoids genistein or naringenin. A mutant of nodD2, tacking 60bp at its 3’end, activated nodC in the presence of inducer, but was defective in regulating certain of the nodD genes. The nodC gene of R. leguminosarum biovar viciae responded differently to the various nodD genes of R. leguminosarum biovar phaseoli than did the nodC of the latter biovar.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 4 (1990), S. 0 
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: In a strain of Rhizobium leguminosarum biovar phaseoli, three copies of the regulatory nodulation gene nodD were identified on the Sym plasmid and sequenced. Two were closely linked to each other and the third was near, but not adjacent, to the nodABC genes. Each of these nodD genes could correct the Nod defect of a nodD mutant strain of R. leguminosarum biovar viciae on peas. A truncated form of nodD2 could also correct this mutant, indicating that the C-terminus of NodD2 is not needed for inducing activity. Upstream of nodD1 and in the same operon is a newly described gene, nolE, whose product appears to be exported into the periplasm. Close to nodD2 is another gene, nolP, with no known counterpart in other rhizobia. Both nolP and nolE-nodD1 are preceded by ‘nod-box’ sequences and, in the former case, there appear to be two tandemly repeated nod-box sequences. Mutations in each of the nodD genes and in the nolE and nolP genes did not abolish nodulation or nitrogen fixation on beans.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Nodulation ability is plasmid-determined in R. leguminosarum9'12 and several determinants for nodule formation and function may be carried on a single plasmid11'15. We therefore attempted to transfer determinants for nodulation ability from strain 128C53, a Hup+ field isolate of R. ...
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 36 (1980), S. 1239-1240 
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary A simple method for the anchorage-dependent culture of line 10 guinea-pig hepatoma cells is described.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    European journal of clinical pharmacology 39 (1990), S. 405-407 
    ISSN: 1432-1041
    Keywords: Nifedipine ; antipyrine ; interaction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Medicine
    Notes: Summary The influence of 2 weeks oral intake of nifedipine (2×20 mg) on the oxidative metabolism of antipyrine was investigated in 12 normal volunteers, who had 1050 mg antipyrine solution orally before and after the course of nifedipine. There were no statistically significant differences in the saliva pharmacokinetic parameters of antipyrine on both occasions. However, the metabolite profile of antipyrine in urine showed a significant reduction in the amount of norantipyrine excreted after compared to that before nifedipine administration (16.5 vs 19.6%). This may have implications for drugs that share a similar demethylation pathway with norantipyrine.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    European journal of clinical pharmacology 39 (1990), S. 169-171 
    ISSN: 1432-1041
    Keywords: antidepressant ; medifoxamine ; tolerance ; pharmacokinetics healthy volunteers
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Medicine
    Notes: Summary Medifoxamine is a monoamine reuptake inhibiting antidepressant drug. We have investigated its pharmacokinetics in normal healthy volunteers. After an overnight fast, ascending doses of 200, 500, 750 and 1000 mg of medifoxamine were taken orally. Plasma samples were analysed using a specific HPLC method. Medifoxamine was well tolerated and exhibited a first order linear pharmacokinetic profile. It underwent rapid absorption and peak plasma concentrations were achieved about 1.0 h after administration. Thereafter the elimination profile was biphasic with a mean terminal half life less than 3 hours. We found a linear relationship (r=0.80) between administered dose and AUC values for the four doses. High values were obtained for the apparent volumes of distribution and the plasma clearance.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Selection was made for the transposition of the kanamycin resistance transposon Tn5 from a location on the chromosome of R. leguminosarum into a transmissible, bacteriocinogenic plasmid that also carries genes required for the induction of nitrogen-fixing nodules on peas. One hundred and sixty independent insertions into transmissible plasmids were isolated. When these plasmids were transferred by conjugation into a non-nodulating strain, which carries a deletion in one of its resident plasmids, of the 160 isolates tested 14 yielded transconjugants that formed nodules that did not fix nitrogen (Fix-) and in a further 15 cases the transconjugants were unable to form nodules (were Nod-). When transferred to a symbiotically proficient strain (i.e. Nod+ Fix+) none of the transconjugants was symbiotically defective; thus the mutations were not dominant. When kan was transduced from the clones that generated Fix- transconjugants into a Fix+ recipient the majority of transductants inherited Fix- indicating that the insertion of Tn5 had induced the symbiotic mutations. Transduction of kan, from the clones that failed to donate Nod+ by conjugation to strain 6015, occurred at barely detectable frequencies and it was not possible to demonstrate transduction of Nod-. kan was co-transduced with Nod+ from some of the clones and some of these transductants also inherited the ability to produce medium bacteriocin and to transfer at high frequency by conjugation. Thus the genes for all these characters are closely linked.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Inflammation 4 (1980), S. 9-25 
    ISSN: 1573-2576
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Rabbit prekallikrein (RPK) was purified from rabbit plasma by ion exchange and lectin column chromatography and preparative polyacrylamide gel electrophoresis. A 1500-fold purification was routinely achieved with a final yield of 5–10%, The purified RPK was found to be a glycoprotein with an apparent molecular weight of 88,000. Activation of RPK with either trypsin or rabbit Hageman factor (active) occurs by limited proteolytic cleavage, producing two disulfide-linked polypeptide chains with molecular weights of 55,000 and 35,000. Both chains contain carbohydrate and the 35,000-molecular-weight polypeptide was shown to incorporate [3H]DFP. Activation of RPK in kaolin-treated plasma was shown to proceed by an analogous mechanism yielding 55,000- and 35,000-molecular-weight polypeptide chains.
    Type of Medium: Electronic Resource
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