Library

X
feed icon rss

Your email was sent successfully. Check your inbox.

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

Proceed reservation?

Export
  • 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
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Expression, isolation and properties of Fur (ferric uptake regulation) protein ofEscherichia coli K 12 (1988)
    Springer
    BioMetals 1 (1988), S. 62-68 
    Details
    ISSN: 1572-8773
    Keywords: Fur repressor ; Iron regulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary The clonedfur (ferric uptake regulation) gene ofEscherichia coli K12 was ligated to an expression vector which was inducible with nalidixic acid. The Fur protein was isolated in a single step by immobilized metal-ion-affinity chromatography over zinc iminodiacetate agarose. The amino acid composition of the isolated protein agreed with that predicted from the gene sequence and indicated post-transcriptional removal of the N-terminal methionine residue. All four cysteines were shown to be present as thiols. Proteolysis with trypsin and chymotrypsin yielded large fragments identifiable on polyacrylamide gel electrophoresis. Various divalent metal ions were found by a nitrocellulose filter binding assay to effect non-specific interaction of the Fur dimer with DNA with a dissociation constant of 7 × 10−12 M. A much smaller value, 2.5 × 10−17 M, was measured by gel mobility retardation assay for binding of Fur to a DNA fragment containing the operator sequences of the aerobactin promoter.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01128019
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...