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  • 1990-1994
  • 1980-1984  (4)
  • 1920-1924
  • 1980  (4)
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  • 1990-1994
  • 1980-1984  (4)
  • 1920-1924
Year
  • 1
    Electronic Resource
    Electronic Resource
    Co-transfer of determinants for hydrogenase activity and nodulation ability in Rhizobium leguminosarum (1980)
    [s.l.] : Nature Publishing Group
    Nature 288 (1980), S. 77-79 
    Details
    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
    URL: http://dx.doi.org/10.1038/288077a0
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Anchorage-dependent culture of line 10 guinea-pig hepatoma cells (1980)
    Springer
    Cellular and molecular life sciences 36 (1980), S. 1239-1240 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF01976152
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    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Isolation of symbiotically defective mutants in Rhizobium leguminosarum by insertion of the transposon Tn5 into a transmissible plasmid (1980)
    Springer
    Molecular genetics and genomics 178 (1980), S. 185-190 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF00267228
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Rabbit prekallikrein (1980)
    Springer
    Inflammation 4 (1980), S. 9-25 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF00914099
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    Paper (German National Licenses)
    Fulltext
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