ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
  • Articles  (2)
  • 27.50.+e  (1)
  • Direction of translation  (1)
  • Deutschland
  • Springer  (2)
  • Cambridge University Press
  • ZBW - Deutsche Zentralbibliothek für Wirtschaftswissenschaften, Leibniz-Informationszentrum Wirtschaft Kiel, Hamburg
Collection
  • Articles  (2)
Publisher
  • Springer  (2)
  • Cambridge University Press
  • ZBW - Deutsche Zentralbibliothek für Wirtschaftswissenschaften, Leibniz-Informationszentrum Wirtschaft Kiel, Hamburg
Years
Topic
  • 1
    ISSN: 1432-0983
    Keywords: Genetic mapping ; Mutant polypeptides ; Direction of translation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Genetic and biochemical studies have been performed with 110 mutants which are defective in cytochrome a·a3 and map in the regions on mit DNA previously designated OXI1 and OXI2. With 88 mutations allocated to OXI1 fine structure mapping was achieved by the analysis of rho − deletions. The order of six groups of mutational sites (A 1, A2, B 1, B2, C 1, C2) thus determined was confirmed by oxi i x oxi j recombination analysis. Analysis of mitochondrially translated polypeptides of oxil mutants by SDS-polyacrylamide electrophoresis reveals three classes of mutant patterns: i) similar to wild-tpye (19 mutants); ii) lacking SU II of cytochrome c oxidase (53 mutants); iii) lacking this subunit and exhibiting a single new polypeptide of lower Mr (16 mutants). Mutations of each of these classes are scattered over the OXI1 region without any detectable clustering; this is consistent with the assumption that all oxil mutations studied are within the same gene. New polypeptides observed in oxil mutants of class iii) vary in Mr in the range from 10,500 to 33,000. Those of Mr 17,000 to 33,000 are shown to be antigenically related to subunit II of cytochrome c oxidase. Colinearity is established between the series of new polypeptides of Mr values increasing from 10,500 to 31,500 and the order of the respective mutational sites on the map, e.g. mutations mapping in A 1 generate the smallest and mutations mapping in C2 the largest mutant fragments. From these data we conclude that i) all mutations allocated to the OXI1 region are in the same gene; ii) this gene codes for subunit II of cytochrome c oxidase; iii) the direction of translation is from CAP to 0X12. Out of 19 mutants allocated to OXI2 three exhibit a new polypeptide; these and all the other oxi2 mutants lack subunit III of cytochrome oxidase. This result provides preliminary evidence that the OXI2 region harbours the structural gene for this subunit III.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 2
    ISSN: 1434-601X
    Keywords: 27.50.+e ; 29.30.Dn
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract This paper reports on precision measurements of conversion lines in the decay of83mKr with nuclear transition energies of 32.1 keV and 9.4 keV, respectively. The spectra were taken from a submonolayer surface of83m Kr frozen onto a cold backing, using the new Mainz solenoid retarding spectrometer. The high luminosity and resolution of this instrument enables the observation of all allowed conversion lines up to theN-shell and to fully separate the elastic component from inelastic satellites. The combined analysis of the data yields the transition energiesE y=32151.5±1.1 eV and 9405.9±0.8 eV, respectively. The experiment served also to pilot the application of this spectrometer to the question of a finite neutrino rest mass, searched for in theβ-decay spectrum of tritium and to problems in precision electron spectroscopy in general.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...