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  • 1990-1994  (2)
  • Ferritin  (1)
  • iron  (1)
  • Analytical Chemistry and Spectroscopy
  • Chemistry
  • Polymer and Materials Science
Source
Material
Years
Year
Keywords
  • 1
    Electronic Resource
    Electronic Resource
    A brief history of iron metabolism (1991)
    Springer
    BioMetals 4 (1991), S. 1-6 
    Details
    ISSN: 1572-8773
    Keywords: Cell respiration ; Cytochromes ; Ferritin ; Transferrin receptor ; Siderophores
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary A concise history of selected aspects of iron metabolism is presented. According to present understanding, the element is known to be required for transport and reduction of O2, for reduction Of CO2, N2 and ribonucleotides, and for other essential cellular processes. The contributions of pioneers in the field, preeminent among them the cell physiologist and biochemist Otto Warburg, are recounted.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01135550
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Site-directed mutagenesis of the ferric uptake regulation gene of Escherichia coli (1994)
    Springer
    BioMetals 7 (1994), S. 292-298 
    Details
    ISSN: 1572-8773
    Keywords: iron ; mutagenesis ; repressor
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The 12 histidine and four cysteine residues of the Fur repressor of Escherichia coli were changed, respectively, to leucine and serine by site-directed mutagenesis of the fur gene. The affects of these mutations were measured in vivo by ligation of the mutated genes to a wild-type fur promoter followed by measurement of the ability of these plasmids to regulate expression of a lacZ fusion in the aerobactin operon. In vitro affects were assayed by insertion of the mutated genes in the expression vector pMON2064 attended by isolation of the altered Fur proteins and appraisal of their capacity to bind to operator DNA. The results suggest that cysteine residues at positions 92 and 95 are important for the activity of the Fur protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00144124
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
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