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Interaction of human α-lactalbumin with fatty acids: Determination of binding parameters

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Abstract

The interaction of holo-and apo-forms of human α-lactalbumin with fatty acids was studied by a partition equilibrium method. Apo-α-lactalbumin, obtained by treatment with EDTA, displays one binding site for fatty acids, the association constants for oleic and palmitic acids being 1.9·106 and 4.2·105 M−1, respectively. However, holo-α-lactalbumin was unable to bind fatty acids as measured by this technique. Likewise, no fatty acids bound to holo-α-lactalbumin, isolated using nondenaturing conditions, were detected by gas chromatography. These results demonstrate that the conformational change induced in α-lactalbumin by the removal of calcium enables the protein to interact with fatty acids.

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Authors and Affiliations

  1. Tecnologia y Bioquimica de los Alimentos, Facultad de Veterinaria, Universidad de Zaragoza, Miguel Servet, 177, 50013, Zaragoza, Spain

    C. Barbana, M. D. Perez, C. Pocovi, L. Sanchez & Z. Wehbi

Authors
  1. C. Barbana
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  2. M. D. Perez
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  3. C. Pocovi
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  4. L. Sanchez
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  5. Z. Wehbi
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Correspondence to C. Barbana.

Additional information

Published in Russian in Biokhimiya, 2008, Vol. 73, No. 6, pp. 886–892.

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Barbana, C., Perez, M.D., Pocovi, C. et al. Interaction of human α-lactalbumin with fatty acids: Determination of binding parameters. Biochemistry Moscow 73, 711–716 (2008). https://doi.org/10.1134/S0006297908060126

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  • DOI: https://doi.org/10.1134/S0006297908060126

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