Skip to main content
SpringerLink
Log in

An Equilibrium and a Kinetic Stopped-Flow Fluorescence Study of the Binding of Various Metal Ions to Goat Alpha-Lactalbumin

  • Original Paper
  • Published:
Journal of Fluorescence Aims and scope Submit manuscript

Abstract

Various metal ions bind to the protein α-lactalbumin prepared from goat milk. The stability of the protein after metal binding is compared with that of the apo-protein by monitoring the fluorescence of the tryptophan residues under equilibrium conditions. The kinetics of the metal binding is studied by stopped-flow fluorescence spectroscopy. By means of the Arrhenius plots, the activation energy with regard to the binding of the different ions is determined.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Fig. 1
Fig. 2
Fig. 3
Fig. 4
Fig. 5
Fig. 6

Similar content being viewed by others

References

  1. Pike ACW, Brew K, and Acharya KR (1996). Crystal structures of guinea-pig, goat and bovine α-lactalbumin highlight the enhanced conformational flexibility of regions that are significant for its action in lactose synthase. Structure 4, 691–703.

    Article  PubMed  CAS  Google Scholar 

  2. Kronman MJ (1989). Metal-ion binding and the conformational properties of α-lactalbumin. CRC Crit. Rev. Biochem. Mol. Biol. 24, 565–667.

    CAS  Google Scholar 

  3. Permyakov SE, Veprintsev DB, Brooks CL, Permyakov EA, Berliner LJ (2000). Zinc binding in bovine α-lactalbumin: Sequence homology may not be a predictor of subtle functional features. Proteins: Struct. Funct. Genet. 40, 106–111.

    Article  CAS  Google Scholar 

  4. Permyakov EA, Berliner LJ (2000). α-lactalbumin: structure and function. FEBS Lett. 473, 269–274.

    Article  PubMed  CAS  Google Scholar 

  5. Noyelle K, Van Dael H (2001). Kinetics of conformational changes induced by the binding of various metal ions to bovine α-lactalbumin. J. Inorg. Bioch. 88, 69–76.

    Article  Google Scholar 

  6. Permyakov EA, Berliner LJ (1994). Co2+ binding to α-lactalbumin. J. Prot.Chem. 13, 277–281.

    Article  CAS  Google Scholar 

  7. Vanhooren A (2005). Effects of heat and of near-UV irradiation on goat α-lactalbumin. PhD Thesis.

  8. Vanhooren A, Devreese B, Vanhee K, Van Beeumen J, Hanssens I (2002). Photoexcitation of tryptophan groups induces reduction of two disulfide bonds in goat α-lactalbumin. Biochemistry 41, 11035–11043.

    Article  PubMed  CAS  Google Scholar 

  9. Ren J, Stuart DI, Acharya KR (1993). α-lactalbumin possesses a distinct zinc binding site. J. Biol. Chem. 268, 19292–19298.

    PubMed  CAS  Google Scholar 

  10. Murakami K, Berliner LJ (1983). A distinct zinc binding site in the α-lactalbumins regulates calcium binding. Is there a physiological role for this control? Biochemistry 22, 3370–3374.

    Article  PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Interdisciplinary Research Centre, K.U. Leuven Campus Kortrijk, Sabbelaan 53, 8500, Kortrijk, Belgium

    H. Van Dael & A. Chedad

Authors
  1. H. Van Dael
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. A. Chedad
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to H. Van Dael.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Van Dael, H., Chedad, A. An Equilibrium and a Kinetic Stopped-Flow Fluorescence Study of the Binding of Various Metal Ions to Goat Alpha-Lactalbumin. J Fluoresc 16, 361–365 (2006). https://doi.org/10.1007/s10895-006-0066-z

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s10895-006-0066-z

Keywords

Search

Navigation