text: Interaction of human alpha-lactalbumin with fatty acids: determination of binding parameters.
  The interaction of holo- and apo-forms of human alpha-lactalbumin with fatty acids was studied by a partition equilibrium method. Apo-alpha-lactalbumin, obtained by treatment with EDTA, displays one binding site for fatty acids, the association constants for oleic and palmitic acids being 1.9.10(6) and 4.2.10(5) M(-1), respectively. However, holo-alpha-lactalbumin was unable to bind fatty acids as measured by this technique. Likewise, no fatty acids bound to holo-alpha-lactalbumin, isolated using nondenaturing conditions, were detected by gas chromatography. These results demonstrate that the conformational change induced in alpha-lactalbumin by the removal of calcium enables the protein to interact with fatty acids.
entities.id: T10 T11 T12 T13 T14 T1 T2 T3 T4 T5 T6 T7 T8 T9
entities.type: GENE-Y GENE-Y GENE-Y GENE-Y GENE-Y CHEMICAL CHEMICAL CHEMICAL CHEMICAL CHEMICAL CHEMICAL CHEMICAL CHEMICAL GENE-Y
entities.text: holo-alpha-lactalbumin human alpha-lactalbumin holo-alpha-lactalbumin alpha-lactalbumin human alpha-lactalbumin EDTA fatty acids oleic and palmitic acids fatty acids fatty acids calcium fatty acids fatty acids Apo-alpha-lactalbumin