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
    Copper binding and release by immobilized transferrin: A new approach to heavy metal removal and recovery (1997)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 53 (1997), S. 01-09 
    Details
    ISSN: 0006-3592
    Keywords: transferrin ; conalbumin ; metalloprotein ; affinity chromatography ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Recently these laboratories have demonstrated that it is possible to use proteins as efficient, selective agents for heavy metal removal and recovery. In this study, transferrin was chemically bound to an insoluble support. The ability of immobilized transferrin to produce clean water was demonstrated. Copper loading was independent of feed concentration. The loaded copper could be readily eluted and concentrated into the gram per liter range. The mechanism of copper release was studied. It was shown that release was dependent on pH and the chelating ability of the stripping agent. Metal release occurred slowly at pH 〈 7. However, at low pH in the presence of a chelator, metal removal occurred much more efficiently. The binding constant of copper to immobilized transferrin was determined as a function of pH. This information was used to model metal binding and release to the protein/support matrix. © 1997 John Wiley & Sons, Inc.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
  • 2
    Electronic Resource
    Electronic Resource
    Transferrin metalloprotein affinity metal chromatography (1995)
    Chichester : Wiley-Blackwell
    Journal of Chemical Technology AND Biotechnology 62 (1995), S. 373-379 
    Details
    ISSN: 0268-2575
    Keywords: transferrin ; affinity chromatography ; metalloprotein ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: The metal transport protein transferrin, when immobilized to Sepharose, can serve as an affinity media for the selective removal and subsequent release of heavy metal ions from aqueous solution. The material is stable over the pH range of 2-10, is self-indicating for the binding of certain metal ions, and maintains its integrity towards metal-binding capacity for long periods of time. In one step heavy metal ion concentrations can be reduced by at least five orders of magnitude to, at most, part per billion levels. The findings here presented suggest a novel practical method for the decontamination and/or recovery of metals ions from very dilute solutions and represent the first efforts to extend the concept of affinity chromatography to metal ions.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jctb.280620410
    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...