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  • Arginine  (1)
  • Raguinite  (1)
  • 1975-1979  (2)
  • 1945-1949
  • 1979  (2)
  • 1948
  • 1
    Electronic Resource
    Electronic Resource
    Die Kristallstruktur von TlFeSe2 und TlFeS2 (1979)
    Springer
    Monatshefte für Chemie 110 (1979), S. 1045-1055 
    Details
    ISSN: 1434-4475
    Keywords: Chalcogenides ; Crystal structure ; Raguinite ; TlFeS2 ; TlFeSe2
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract TlFeSe2 is monoclinic, space groupC2/m−C 2h 3 ,a=11.973 Å,b=5.490 Å,c=7.110 Å, β=118.2°,Z=4. TlFeS2 is isotypic witha=11.636 Å,b=5.304 Å,c=6.799 Å, β=116.7°. The crystal structure of TlFeSe2 has been determined from single crystal diffractometer data. Isotypy of the sulfide has been confirmed from powder diffraction data. The crystal structure containing infinite linear chains of edgesharing FeX 4-tetrahedra, and its relationship to the thio- and selenoferrates of the alkali metals are discussed. The mineral raguinite is very probably isotypic to synthetic TlFeS2.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00910952
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  • 2
    Electronic Resource
    Electronic Resource
    Sequestration of arginine by polyphosphate in vacuoles of yeast (Saccharomyces cerevisiae) (1979)
    Springer
    Archives of microbiology 121 (1979), S. 169-175 
    Details
    ISSN: 1432-072X
    Keywords: Yeast ; Vacuoles ; Compartmentation ; Polyphosphate ; Arginine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Isolated and purified vacuoles from yeast protoplasts contain the bulk of the cellular pool of arginine. The arginine is firmly retained in the isolated vacuoles despite of the presence of a permease which mediates arginine diffusion through the vacuolar membrane (Boller et al., 1975). It is shown, mainly by equilibrium dialysis, on vacuolar extracts, that the retention of arginine in the vacuoles is due to binding by polyphosphate. The polyphosphate appears to be located exclusively in the vacuoles. Enzymes hydrolysing polyphosphate are also located in the vacuoles. Isolated vacuoles from arginine grown cells contain about three times as much polyphosphate as vacuoles from ammonium grown cells; the vacuolar pool of arginine is correspondingly greater. Thus there seems to be a close correlation between the storage of arginine and polyphosphate. This confirms the observation that under conditions provoking “polyphosphate overcompensation” (Liss and Langen, 1962) the accumulation of enormous quantities of polyphosphate is associated with that of corresponding quantities of arginine, provided this amino acid is supplied in the medium. Yet, under certain growth conditions the cells are able to store, and to mobilize, both arginine and polyphosphate independently.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00689982
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