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  • 1995-1999  (4)
  • metalloprotein  (4)
  • transferrin  (2)
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Material
Years
  • 1995-1999  (4)
Year
Keywords
  • 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
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    Paper (German National Licenses)
  • 2
    Electronic Resource
    Electronic Resource
    Immobilization of conalbumin onto polystyrene/divinylbenzene co-polymers: Towards finding the best support for MAMC (1996)
    Chicester [u.a.] : Wiley-Blackwell
    Journal of Molecular Recognition 9 (1996), S. 558-563 
    Details
    ISSN: 0952-3499
    Keywords: conalbumin ; affinity chromatography ; metal ; metalloprotein ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Immediately after the successful immobilization of conalbumin onto CNBr-activated Sepharose, efforts were begun to find a less expensive support and a more benign chemistry of activation. The potential of the Sepharose-conalbumin conjugate for decontamination of several metal-containing waste-waters has been established, and a new method of chromatography has emerged, named metalloprotein affinity metal chromatography (MAMC). Efforts to immobilize conalbumin onto polystyrene/divinylbenzene co-polymers, using the well known and commercially available Merrifield, aminomethyl and plain polystyrene resins are presented here. Immobilizations of conalbumin were carried out on the Merrifield and Aminomethyl resins, but the procedures were time consuming and complicated by polymer aggregation. Because of high cost of these materials, research was directed towards the activation and functionalization of plain polystyrene/divinylbenzene co-polymers. Chlorosulfonation followed by sulfonamide formation was attempted on three commercially available polymers. Successful polysulfonamide formation was achieved with bislysine copper(II) acting as a diamine. Removal of the copper allows the unblocking of the α amino group of the immobilized lysine which in turn is treated with glutaraldehyde, afforing an activated support for immobilization of proteins. To date, approximately 46 mg transferrin/g dry matrix have been successfully immobilized. The chemical and biological inertness of this support makes it a good candidate to scale up the procedure and continue the optimization of MAMC.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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    Paper (German National Licenses)
  • 3
    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
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Use of thermolysin metalloprotein affinity metal chromatography in the decontamination of actinide-bearing solutions (1995)
    Chichester : Wiley-Blackwell
    Journal of Chemical Technology AND Biotechnology 64 (1995), S. 149-152 
    Details
    ISSN: 0268-2575
    Keywords: thermolysin ; affinity chromatography ; metalloprotein ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Thermolysin metalloprotein affinity metal chromatography (MAMC) has been shown to be effective for the removal and concentration of lanthanide and actinide ions from aqueous solution. Using solution of trivalent lanthanide ions of appropriate radii and of Th4+ and UO22+ ions as models, the calciumbinding sites of immobilized thermolysin have shown appreciable potential for the decontamination of actinide-bearing waster solutions. The zinc-binding site of the affixed protein may also be used for the removal and concentration of divalent transition metal ions.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jctb.280640206
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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